Revised as of April 8, 2020 (SEE p.8)
2020-2021
Graduate School of Biostudies, Kyoto University

Master’s Program in “Global Frontier in Life Science”
Guidelines for International Student Admissions
Philosophy and Admission Policy of the Graduate School of Biostudies
As an advanced discipline that holds the key to the future of humankind, the life sciences today are
undergoing a major evolutionary change. In response to this global trend, the Graduate School of
Biostudies was founded in 1999 as Japan’s first independent graduate school focused on the life
sciences with the objective of building a world-class center for research and developing individuals
who can lead the life sciences field into the next generation. Our school has engineered a true fusionof cutting-edge areas in several existing fields. By harnessing the common language of “cells,
molecules, and genes” that together form the fundamental principles of life, we have developed an
integrated understanding of diverse life forms and the environments they help shape, and havelaunched innovative efforts in research and education that will produce a new set of values for the
future and dignity of life.
To meet the diverse expectations of society for advances in the life sciences, which are becoming
increasingly sophisticated and complex, our school seeks students from a broad spectrum of
backgrounds who share these ideals of our school, who possess basic academic skills and research
aptitudes in the life sciences, and who demonstrate a strong sense of ethics and responsibility intheir academic research. We especially welcome students who possess a pioneering spirit to help
propel the comprehensive and advanced branches of the life sciences, free from preconceptions,while fully appreciating the dignity of life. Accordingly, the Graduate School of Biostudies
endeavors to cultivate individuals with the following attributes:
1. Researchers ready to discover, or to shed fresh light on, fundamental principles of life, who will
pioneer new areas of the life sciences;
2. Researchers and engineers committed to global environmental conservation and gains in humanhealth, welfare, and well-being, who are ready to make social contributions through roles in public
and private research institutions;
3. Educators and working professionals with a broad-based understanding of the varied phenomenaof life in general, who are ready to make social contributions through roles in education, industry,
the news media, and government;
4. Researchers, educators, engineers, and working professionals who possess strong communication
skills that enable them to hold discussions with researchers and others from Japan and around theworld in life science–related fields.
The entrance exam will comprise achievement tests that include a written exam to evaluate theapplicant’s ability to think logically in English, a skill that is required to read and analyze an article
published in an international journal; a written exam to assess the applicant’s general knowledge ofmolecular biology, cell biology, biochemistry, and other life science fields; a written exam to assess
the applicant’s fundamental knowledge as required to pursue his or her intended field of study; andan oral exam to assess the applicant’s judgement, thinking ability, communication skills, initiative,and ethical perspective. Admissions decisions will be made based on the applicant’s overall
performance on these exams.
Please note that applicants are NOT required to be physically present in Japan for theexamination.
The academic year starts on October 1, 2020 or April 1, 2021.
1

I. “Global Frontier in Life Science”
The Graduate School of Biostudies launched “Global Frontier in Life Science”, an educational
program for Doctoral and Master’s students, as a part of K.U. PROFILE (Kyoto University
Programs for Future International Leaders: http://www.opir.kyoto-u.ac.jp/kuprofile/e/index.html).
This program, “Global Frontier in Life Science”, is held entirely in English, including the entrance
examinations, lectures, experiments, and discussions. Up to ten applicants will be accepted.

II. Division/Laboratories and Enrollment
The Graduate School of Biostudies consists of two divisions, which are made up of 41 laboratories.
Details of each laboratory are described on pp. 10 - 32 of these guidelines and the Graduate Schoolof Biostudies website (http://www.lif.kyoto-u.ac.jp/). Applicants can apply for up to twolaboratories. Thus, applicants must contact the lab heads and fully discuss potential research
activities and availability before filing the application.

III-1. Eligibility Requirements for Applicants expecting to start from October
1, 2020
Applicants must match one of the following requirements by September 30, 2020:
1. Individuals with any nationality who have completed (or are expected to complete by
September 30, 2020) 16 years of education in foreign countries. This includes individuals
who have completed an equivalent of 16 years of education but have less than 16 years due
to skipped (advanced) grades.
2. Individuals, other than Japanese nationals, who graduated (or are expected to graduate by
September 30, 2020) from a Japanese university.
3. Individuals who have received (or are expected to receive by September 30, 2020) a degree
equivalent to a bachelor’s degree by completing a curriculum with a term of enrollment of atleast three years (including completion of such a curriculum by studying relevant subjects inJapan via a correspondence course provided by a school in a foreign country and completionof a curriculum at an educational facility that has been accredited as having an approved
curriculum under the educational system of said country and is designated by the Minister of
Education, Culture, Sports, Science and Technology) at a university or other school in acountry other than Japan (only those universities or schools for which the overall conditionsof education and research activities have been assessed by a party authorized by thegovernment of said country or an organization concerned, or those corresponding to such
entities as designated by the Minister of Education, Culture, Sports, Science and Technology).
4. Individuals, other than Japanese nationals, who are recognized by the Graduate School of
Biostudies to have completed an education equivalent to a university degree of Japan and areat least 22 years old by September 30, 2020.
5. Individuals with Japanese nationality who are determined by the Graduate School of
Biostudies to have completed an education in foreign countries equivalent to a university
degree of Japan or had school education that were mainly given in English, and are at least
22 years old by September 30, 2020.
Those who are applying under requirement 4 or 5 must undergo a preliminary eligibility
screening process before applying.
2

III-2. Eligibility Requirements for Applicants expecting to start from April 1,
2021
Applicants must match one of the following requirements by March 31, 2021:
1. Individuals with any nationality who have completed (or are expected to complete by March
31, 2021) 16 years of education in foreign countries. This includes individuals who havecompleted an equivalent of 16 years of education but have less than 16 years due to skipped(advanced) grades.
2. Individuals, other than Japanese nationals, who graduated (or are expected to graduate by
March 31, 2021) from a Japanese university.
3. Individuals who have received (or are expected to receive by March 31, 2021) a degree
equivalent to a bachelor’s degree by completing a curriculum with a term of enrollment of atleast three years (including completion of such a curriculum by studying relevant subjects inJapan via a correspondence course provided by a school in a foreign country and completionof a curriculum at an educational facility that has been accredited as having an approved
curriculum under the educational system of said country and is designated by the Minister of
Education, Culture, Sports, Science and Technology) at a university or other school in acountry other than Japan (only those universities or schools for which the overall conditionsof education and research activities have been assessed by a party authorized by thegovernment of said country or an organization concerned, or those corresponding to such
entities as designated by the Minister of Education, Culture, Sports, Science and Technology).
4. Individuals, other than Japanese nationals, who are recognized by the Graduate School of
Biostudies to have completed an education equivalent to a university degree of Japan and areat least 22 years old by March 31, 2021 .
5. Individuals with Japanese nationality who are determined by the Graduate School of
Biostudies to have completed an education in foreign countries equivalent to a university
degree of Japan or had school education that were mainly given in English, and are at least
22 years old by March 31, 2021.
6. Individuals, other than Japanese nationals, who will be enrolled at least 3 years in a Japanese
university by March 31, 2021 and are recognized by the Graduate School of Biostudies as
having acquired sufficient credits with excellent academic records.
Those who are applying under requirement 4 or 5 must undergo a preliminary eligibility
screening process before applying.

IV. Eligibility Screening
Applicants filing under eligibility requirement 4, 5, or 6 above are required to contact the Student
Affairs Section (Kyomu gakari) of the Graduate School of Biostudies to request that the designatedapplication form for preliminary eligibility screening to be sent at any time, but no later than April
9 (Thu), 2020. Submit the following preliminary eligibility screening documents via email to theStudent Affairs Section of the Graduate School of Biostudies (150kyomu@adm.lif.kyoto-u.ac.jp)
by JST 5:00 p.m., April 16 (Thu), 2020 at latest. When filing the admission application, applicantscannot in principle apply for any laboratory other than the one or two specified in the documents
being submitted for the eligibility screening.
The screening results will be sent by e-mail to the applicants as soon as the decision is made, atlatest on May 14 (Thu), 2020.
3

1. Documents for the Eligibility Screening
When filing under eligibility requirement 4 or 5
(1) Application form for theeligibility screening(designated form)(2) Academic transcript(3) Research progress report(designated form)(4) Details of previous studies(designated form)(5) A valid score for GRE
General Test or Subject Test
(See Note below)(6) Others

This form is provided upon request.

Submit an academic transcript prepared and sealedby the university last attended. (The transcript does
not need to be sealed if it is made of a material thatprevents photocopying.)
Present a brief, objective statement on the progressof the applicant’s research in the field ofspecialization.
This form is provided upon request.
Submit a certificate of research work content
prepared and sealed by the institution to which theapplicant belongs.
This form is provided upon request.
Any scores of the Subject Test are optional.
Acceptable test includes: Biology/ Biochemistry,
Cell and Molecular/Biology/Chemistry/Physics.
Documents or printed materials that support
academic or scientific achievements, if any, such as
books, research articles, or academic presentations.

When filing under the eligibility requirement 6(1) Application form for theeligibility screening

This form is provided upon request.
(designated form)(2) Letter of recommendation

Submit a letter of recommendation prepared andsealed by the university in which you are/wereenrolled.
Note that recommendation letters must be written
on the letterhead of the institution to which therecommender belongs and are valid only when therecommender's handwritten signature and fullcontact addresses (including Email address) areprovided.
Submit an academic transcript prepared and sealedby the university in which you are/were enrolled.
(The transcript does not need to be sealed if it ismade of a material that prevents photocopying.)
This form is provided upon request.

(3) Academic transcript(4) Statement of personal
objectives (designated form)(5) A valid score for GRE
General Test or Subject Test
See Note below)

Any scores of the Subject Test are optional.
Acceptable test includes: Biology/ Biochemistry,
Cell and Molecular/Biology/Chemistry/Physics.

4

Note
1) For applicants who hold a GRE* General Test or Subject Test score for
Biology/Biochemistry, Cell and Molecular Biology/Chemistry/Physics, those scores canbe provided as supplemental supporting information.
*GRE: Graduate Record Examination http://www.ets.org/gre
Designated Institution (DI) Code: 3814 Kyoto U2) Successful applicants filing under the eligibility requirement 6, expecting to matriculate
in April, 2021, must submit an academic transcript for the 2020 academic year to theStudent Affairs Section (Kyomu gakari) of the Graduate School of Biostudies by February
25 (Thu), 2021. Otherwise successful applicants whose transcripts demonstrate a failure
to meet the admissions standards of the Graduate School of Biostudies may be refused
admission.
Successful applicants filing under eligibility requirement 6 must also submit a certificate
of withdrawal by March 31 (Wed), 2021; thus, they cannot obtain a bachelor’s degree atthe university currently attended.

V. Application Fee
Application fee: 10,000 yen
Payment period: From May 1 (Fri) to May 15 (Fri), 2020 JST
Only payments marked as made within this period will be valid; those made outside thisperiod will be invalid. Once received, application fees will not be refundable under any
circumstances.

[Payment methods]
1. Payment by Credit Card (only for applicants residing outside Japan).
Applicants residing outside Japan should pay the application fee (10,000 yen) and Service
Fee (650 yen). Please access the URL below titled “Examination Settlement Service (EXSS)”and complete the payment process following the instructions provided during the designatedpayment period. For details, please refer to a separate sheet titled “Payment Methods forApplication Fees with Convenience Store or Credit Card”. Note that the Application
Completed page must be printed out and submitted along with the other application
documents (see section VI below).
EXSS: https://www3.univ-jp.com/kyoto-u/en/bio/
2. Payment with Convenience Store (only for applicants residing inside Japan).
Applicants residing inside Japan should pay the application fee (10,000 yen) and Service
Fee (650 yen). Please access the URL below titled “Examination Settlement Service (EXSS)”and complete the payment process following the instructions provided during the designatedpayment period. For details, please refer to a separate sheet titled “Payment Methods forApplication Fees with Convenience Store or Credit Card”. Note that the Application
Completed page must be printed out and submitted along with the other application
documents (see section VI below).
EXSS: https://www3.univ-jp.com/kyoto-u/en/bio/5

3. Payment by bank transfer (only for applicants residing inside Japan).
Applicants residing inside Japan should pay the application fee (10,000 yen) by banktransfer with the following procedures.
Payment at a bank window in Japan(1) Enter the applicant’s name in the appropriate spaces (three spaces) on the
Application Fee Payment Request Form (available upon request via regularmail). Take the form to a bank without separating any of its portions (payment
through the post office or Japan Post Bank is not available) and make yourpayment. Please note that payment via the Internet is not accepted.
(2) No transfer fee is charged if payment is made at the head office or a branch office of
Mitsui Sumitomo Banking Corporation. If payment is made at any other bank, you
shall be responsible for the cost of transfer.
(3) After making your payment, make sure that the bank’s receipt seal is stamped on the“Evidence of Application Fee Payment” and the “Application Fee (and Transfer Fee)
Receipt” returned from the bank. Paste the “Evidence of Application Fee Payment”(left portion) on the “Form for Affixing Evidence of Application Fee Payment”.
Please retain the copy of the “Application Fee (and Transfer Fee) Receipt” withrevenue stamp attached for your records.
Payment via ATM
Bank Name

BranchType of Account

Mitsui Sumitomo Bank

Kyoto

Ordinary (futsu)

三井住友銀行

京都支店

普通Account No.

8089428

Recipient’s Name

Kyoto University
国立大学法人 京都大学

(1) Enter the applicant’s name as the payer in the appropriate space in the ATM so that theuniversity will be able to identify by whom the amount was deposited in theuniversity’s account.
(2) Extra charge for deposit via ATM must be paid by the applicant.
(3) Submit the receipt of the deposit to be issued with the ATM and make a photocopyof the receipt for yourself.

VI. Application Documents(1) Admission application form, Use the provided form.
photograph card,
Fill in the blanks and paste a photo to each of the two indicatedexamination card
places. Make sure the photos present your full-face and frontal
view, without a hat or cap, and are taken within the past threemonths.
(2) Research achievement
Use the provided form.
(Questions for application
Fill in the boxes in the designated form. Do not exceed to write
screening)
expanding the original size of the boxes. The sizes are fixed. Pleasewrite in Times New Roman 12 point.
(3) Academic transcript
Submit an academic transcript prepared and sealed by the university
you are currently attending or from which you have graduated.

6(4) Graduation certificate(or certificate of expectedgraduation)(5) Recommendation letters

Submit a certificate prepared by the university you are currently
attending or from which you have graduated.
At least two letters are required.
(Mandatory)
Letter of recommendation 1:
Written by a faculty member of your current educational
institution, who can evaluate your academic performance andpotential for success in the Master’s program. The letter must be
written on the letterhead of the respective institution and must
include the recommender's contact information and handwritten signature.

(Choose at least one, as appropriate)
Letter of recommendation 2:
Written by the faculty supervisor of the applicant at theuniversity to which you belong or from which you graduated,
who can evaluate your research and your potential to becomea productive scientist. The letter must be written on theletterhead of the supervisor's institution and must include thesupervisor's contact information and hand-written signature.
Letter of recommendation 3:
If you are employed at a public agency or company at the timeof application, submit a letter of recommendation from yourimmediate supervisor, with his/her hand-written signature. The
letter must include your supervisor's contact information andbe written on the letterhead of the agency/company to which
he/she belongs.
(6) A valid score for GRE
General Test score is required.
General Test and Subject Test Any scores of the Subject Test are optional. Acceptable test includes:
Biology/Biochemistry, Cell and Molecular/Biology/Chemistry/Physics(7) A valid score for IELTS or
Unnecessary for English-native speakers (Please contact the Student
TOEFL
Affairs Section in advance.)(8) Evidence of application fee
payment form

(9) Address forfurther communication

Applicants residing outside Japan: After paying your application
fees via internet, the Application Completed page must be printed out
and submitted. Applications will not be accepted if payment could not
be confirmed.
Applicants residing inside Japan: After paying your application fees at
a convenience store or a bank window or by an ATM, paste the
Evidence of Application Fee Payment with the bank’s receipt seal
stamped or the receipt issued by the ATM. Applications will not be
accepted if no receipt seal is stamped on the Evidence of Application
Fee Payment form.
Use the designated forms.
For further communication on the examination results and theenrollment procedures, clearly write your name, address and post codeon the designated form.

7

*If you change your address after applying, you must promptly informthe new address to the Student Affairs Section (Kyomu gakari) of the
Graduate School of Biostudeis.

VII. Application Procedures
Applicants must prepare a packet of all necessary admission application documents in print andsubmit it to the postal address indicated on p.9. When sending the packet by post, use registeredmail and write clearly “Admission Application Form for the Graduate School of Biostudies Master’s
program of Global Frontier in Life Science” on the front of the envelope.

VIII. Application Period
The application period is from May 18 (Mon) to May 22 (Fri), 2020 JST.
When submitting in person: office hours are 9:00 a.m. – 12:00 p.m. and 1:00 p.m. – 5:00 p.m.
When sending the application documents by post, ensure that the application documents aredelivered by JST 5:00 p.m. on May, 22 (Fri), 2020.
Note that the admission application form will not be accepted if the application completed page orthe Evidence of Payment for Application Fees with the bank’s receipt seal stamped or the receipt
issued by the ATM is not pasted on the Form for Affixing Evidence of Payment for Application
Fees.

--- Revision (as of April 8, 2020) ----------------------------------------------------------1) If you are unable to submit a GRE General Test score or a TOEFL/IELTS score by May 22,2020 due to your local test schedule change concerning the COVID-19 coronavirus epidemic,
later submissions will be accepted until June 30, 2020.
In this case, please notify the Student Affairs Section of the Graduate School of Biostudies ofyour situation, no later than May 22, 2020.
2) Before enclosing your application documents, please make a scanned copy (pdf) of them andsend them to the Student Affairs Section (150kyomu@adm.lif.kyoto-u.ac.jp) via email so that the
copy can be substituted if your documents sent by post did not arrive in our office by thedesignated deadline.
--------------------------------------------------------------------------------------------------------------------------IX. Examination Schedule
June 1 (Mon)~

June 5 (Fri)

June 17 (Wed)~July 10 (Fri)Documentation Screening
Only successful applicants who pass the screeningof the admission documents will be able to take theinterview (Oral Examination).
Interview (Oral Examination)
The interview date and method* will be arranged
individually after the decision is made.
*e.g. Skype or other protocols

8

X. Announcement of Successful Applicants
The list of successful applicants is scheduled to be posted on a bulletin board on the 1st floor of
the South Campus Research Bldg. (Faculty of Medicine Bldg. G) at approximately 5p.m., July 22(Wed), 2020. Simultaneously, the same list will be posted on the web site of the Graduate Schoolof Biostudies (http://www.lif.kyoto-u.ac.jp/e/). Telephone inquiries about the selection results shallnot be accepted.

XI. Admission Fee and Tuition
Admission Fee: 282, 000 yen (tentative)(The admission fee amount may be revised at the time of enrollment.)
Tuition for the first semester: 267,900 yen (annual tuition: 535,800 yen, tentative)(The tuition fee amount may be revised at the time of enrollment or later.)

Notes:(1) “Master’s Program” at Kyoto University refers to the first two-year program in a doctoral
program specified in the Standards for the Establishment of Graduate Schools, and is a term used
at Kyoto University.
(2) Students who have completed the Master's degree in the Graduate School of Biostudies and wish
to continue on for the Doctoral Program must nevertheless submit a formal application for theDoctoral Program.
(3) Others
1) After the application is accepted, no changes are allowed in any of the application items.
Furthermore, once received, application fees will not be refundable under any circumstances.
2) For applicants residing inside Japan: To request the Application Fee Payment Request
Form, write your post code, address, and name on a self-addressed 240 mm x 332 mm-sizedenvelope, and affix 80-yen postage to the self-addressed envelope. Write “Request for
Application Fee Payment Request Form” on the front of the envelope, place the selfaddressed envelope inside, and send it to the address below).
3) The instructions of enrollment procedures will be e-mailed to each successful applicant inlate July, 2020 for those who would like to enroll in October, 2020. For those who will enroll
in April, 2021, it will be informed in early February, 2021.
4) Applicants with physical disabilities (degree of physical disability as stipulated in theenforcement ordinance of the School Education Law) who require special arrangements fortaking examinations or attending courses should immediately contact the Student Affairs
Section (Kyomu gakari).
[Handling of Personal Information]
Personal information provided in application documents will be handled in accordance with
“Kyoto University’s Rules regarding the Protection of Personal Information.”9< Notice >From 2021, entrance examinations of the Global Frontier in Life Science will be held inwinter instead of summer. The application period for enrollment in October, 2021 and April,
2022 will begin in December, 2020, and details will be released in September, 2020. Look
for future announcements from the Graduate School of Biostudies.

< Where to send your application, and Inquiries >Student Affairs Section (Kyomu gakari) of the Graduate School of Biostudies,
Kyoto University
Yoshida-Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan
Phone: +81-75-753-9424 Fax: +81-75-753-9229 E-mail: 150kyomu@adm.lif.kyoto-u.ac.jp
December, 2019
Graduate School of Biostudies, Kyoto University
http://www.lif.kyoto-u.ac.jp/e/10

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019

Division of Integrated Life Science
1) Laboratory of Chromosome Transmission
PI: NAKASEKO, Yukinobu (Associate Prof.) <nakaseko@lif.kyoto-u.ac.jp>
Outline of the research
Our research is focused on the cell cycle regulation of eukaryotic cells. Using fission yeast as a model system,
regulation of chromosome segregation and separation during mitosis has been studied. We are trying to identify
individual genes involved in these steps and to elucidate the functional networks of these genes.
Publications
Nakamura, T., Pluskal, T., Nakaseko, Y., and Yanagida, M. Impaired coenzyme A synthesis in fission yeast causes
defective mitosis, quiescence-exit failure, histone hypoacetylation and fragile DNA. Open Biol. 2, 120117 (2012).
doi: 10.1098/rsob.120117.
Irvine, D. V., Goto, D. B., Vaughn, M. W., Nakaseko, Y., McCombie, W. R., Yanagida, M., and Martienssen, R.
Mapping epigenetic mutations in fission yeast using whole-genome next-generation sequencing. Genome Res. 19,
1077-1083 (2009). doi: 10.1101/gr.089318.108.
Hanyu, Y., Imai, K. K., Kawasaki, Y., Nakamura, T., Nakaseko, Y., Nagao, K., Kokubu, A., Ebe, M., Fujisawa, A.,
Hayashi, T., Obuse, C., and Yanagida, M. Schizosaccharomyces pombe cell division cycle under limited glucose
requires Ssp1 kinase, the putative CaMKK, and Sds23, a PP2A-related phosphatase inhibitor. Genes Cells. 14, 539554 (2009). doi: 10.1111/j.1365-2443.2009.01290.x.
Website of the lab: http://www.lif.kyoto-u.ac.jp/e/?post_type=labos&p=135
Key words: chromosome, cell cycle, genetic analysis

2) Laboratory of Gene Biodynamics
PI: SHIRAISHI, Hideaki (Associate Prof.) <siraisi@kuchem.kyoto-u.ac.jp>
Outline of the research
We investigate the growth, morphogenesis, and evolution of photosynthetic microorganisms. We currently focus ondeveloping molecular genetic tools for the analysis and genetic manipulation of the edible alkalophilic
cyanobacterium Arthrospira (Spirulina).
Publications
Shiraishi, H. Cryopreservation of the edible alkalophilic cyanobacterium Arthrospira platensis. Biosci. Biotechnol.
Biochem. 80, 2051-2057 (2016). PMID: 27240586
Shiraishi, H. Association of heterotrophic bacteria with aggregated Arthrospira platensis exopolysaccharides:
implications in the induction of axenic cultures. Biosci. Biotechnol. Biochem. 79, 331-341 (2015). PMID: 25333502
Shiraishi, H. and Tabuse, Y. The Apl I restriction-modification system in an edible cyanobacterium, Arthrospira(Spirulina) platensis NIES-39, recognizes the nucleotide sequence 5’-CTGCAG-3’. Biosci. Biotechnol. Biochem.
77, 782-788 (2013). PMID: 23563565
Website of the lab: http://kuchem.kyoto-u.ac.jp/seika/
Key words: microbiology, cyanobacteria, spirulina, Arthrospira platensis
11Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 20193) Laboratory of Cell Cycle Regulation
PI: ISHIKAWA, Fuyuki (Prof.) < fishikaw@lif.kyoto-u.ac.jp>
Outline of the researchThis laboratory is interested in understanding the mutual interactions between the genome and the surrounding
environment. For example, how do organisms preserve their internal resources until their surrounding conditions are
suitable for reproduction? How do they prevent mortal pathologies such as cancers until they complete growth andreproduction? Is aging a consequence of damage accumulation caused by fluctuating harsh environments? Does theever-changing microenvironments in the wild in contrast to those persistently cultivated in laboratories, play asignificant role, if any, in the life history of an organism in nature? To address these questions, our team branches into
three distinct research teams: telomere group, low-dose stress group, and retrotransposon group.
Publications
Ishikawa, S. and Ishikawa, F. Proteostasis failure and cellular senescence in long-term cultured postmitotic rat neurons. Aging Cell, in press (2019).
Takikawa, M., Tarumoto, Y., Ishikawa, F. Fission yeast Stn1 is crucial for semi-conservative replication at telomeresand subtelomeres. Nucleic Acids Res., 45: 1255-1269 (2017). doi: 10.1093/nar/gkw1176
Chujo, M., Tarumoto, Y., Miyatake, K., Nishida, E. and Ishikawa, F. HIRA, a conserved histone chaperone plays anessential role in low-dose stress response via transcriptional stimulation in fission yeast. J. Biol. Chem. 287: 2344023450 (2012). doi: 10.1074/jbc.M112.349944
Miyake, Y., Nakamura, M., Nabetani, A., Shimamura, S., Tamura, M., Yonehara, S., Saito, M. and Ishikawa, F. RPAlike mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of thePot1 pathway. Mol. Cell 36: 193-206 (2009). doi: 10.1016/j.molcel.2009.08.009
Website of the lab: http://www.lif.kyoto-u.ac.jp/e/?post_type=labos&p=144
Key words: telomere, stress response, retrotransposon

4) Laboratory of Cell Recognition and Pattern Formation
PI: UEMURA, Tadashi (Prof.) <tauemura@lif.kyoto-u.ac.jp>
Outline of the research
1. Nutri-developmental biology: deciphering regulatory systems that govern nutritional adaptability to ensure
animal growth, reproduction, and aging
2. Learning from reproductive parasites: a comprehensive study of “male killing” caused by insect symbionts
3. Neuroscience: operating principles of neuronal circuits that evoke selective behavioral outputs in response tonociceptive stimuli
4. Morphogenesis: common principles of epithelial morphogenesis beyond hierarchies of genome, cells and tissues
We are interested in mechanisms that control animal development and behaviors in response to two categories ofenvironmental inputs: nutrition and sensory stimuli. We are trying to unravel underlying mechanisms of adaptations
to nutrient balances in Drosophila species. We are also taking interspecies approaches to understand contributions ofsymbiotic microorganisms to animal growth and reproductive manipulation (“male killing”). By using Drosophila
somatosensory neurons, we are dissecting operating principles of neuronal circuits that evoke selective behavioral
outputs in response to thermal or mechanical nociceptive stimuli. As a related project, we are interested in how
genomic information and cells cooperatively build up the entire body of an organism, and trying to understandcommon principles of epithelial morphogenesis beyond hierarchies of genome, cells and tissues. To conduct thesestudies, we make full use of molecular, optogenetic, and physiological approaches, imaging, and multi-omics.
12

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Publications
Watanabe, K., Kanaoka, Y., Mizutani, S., Uchiyama, H., Yajima, S., Watada, M., Uemura, T. and Hattori, Y.
Interspecies comparative analyses reveal distinct carbohydrate-responsive systems among Drosophila species.
Cell Reports, 28: 2594-2607.e7 (2019).
Kondo, T. and Hayashi, S. Two-step regulation of trachealess ensures tight coupling of cell fate with morphogenesis in
the Drosophila trachea. eLife, 8: e45145 (2019).
Harumoto, T. & Lemaitre, B. Male-killing toxin in a bacterial symbiont of Drosophila. Nature. 557: 252-255 (2018).
Onodera K., Baba, S., Murakami, A., Uemura, T., and Usui., T Small conductance Ca2+-activated K+ channels induce
the firing pause periods during the activation of Drosophila nociceptive neurons. eLife, 6:e29754 (2017).
Arata, M., Sugimura, S. and Uemura, T. Difference in Dachsous levels between migrating cells coordinates the
direction of collective cell migration. Dev. Cell, 42: 479-498 (2017).
Tsuyama, T., Tsubouch, A., Usui, U., Imamura, H. and Uemura., T. Mitochondrial dysfunction induces dendritic loss
via eIF2α phosphorylation. Journal of Cell Biology, 216: 815-834 (2017).
Website of the lab: http://www.cellpattern.lif.kyoto-u.ac.jp/
Key words: animal development, nutrition, neuroscience, symbiotic microorganisms, morphogenesis, multi-omics

5) Laboratory of Plant Molecular Biology
PI: KOHCHI, Takayuki (Prof.) <tkohchi@lif.kyoto-u.ac.jp>
Outline of the research
1. Photomorphogenesis and environmental regulation of plant development
2. Comparative genomics and molecular genetics with the liverwort, Marchantia polymorpha
3. Genomic and post-genomic analyses of Marchantia polymorpha
Publications
Yamaoka, S., Nishihama, R., Yoshitake, Y., Ishida, S., Okahashi, K., Bao, H., Nishida, H., Yamaguchi, K., Shigenobu, S.,
Ishizaki, K., Yamato, K. T., and Kohchi, T. Generative cell specification requires transcription factors evolutionarily
conserved in land pants. Curr. Biol., 28: 479–486 (2018). doi: 10.1016/j.cub.2017.12.053

Bowman, J.L., Kohchi, T., Yamato, K.T., et al. Insights into land plant evolution garnered from the Marchantia
polymorpha genome. Cell, 171: 287-304 (2017). dx.doi.org/10.1016/j.cell.2017.09.030
Inoue, K., Nishihama, R., Kataoka, H., Hosaka, M., Manabe, R., Nomoto, M., Tada, Y., Ishizaki, K. and Kohchi, T.
Phytochrome signaling is mediated by PHYTOCHROME INTERACTING FACTOR in the liverwort Marchantia
polymorpha. Plant Cell 28: 1406-1421 (2016). doi: 10.1105/tpc.15.01063
Kato, H., Ishizaki, K., Kouno, M., Shirakawa, M., Bowman, J. L., Nishihama, R. and Kohchi, T. Auxin-mediatedtranscriptional system with a minimal set of components is critical for morphogenesis through the life cycle inMarchantia polymorpha, PLOS Genet. 11: e1005084 (2015). doi: 10.1371/journal.pgen.1005084
13

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Komatsu, A., Terai, M., Ishizaki, K., Suetsugu, N., Tsuboi, H., Nishihama, R., Yamato, K. T., Wada, M. and Kohchi, T.
Phototropin encoded by a single-copy gene mediates chloroplast photorelocation movements in the liverwort Marchantia
polymorpha L., Plant Physiol. 166: 411-427 (2014). doi: 10.1104/pp.114.245100
Kubota, A., Kita, S., Ishizaki, K., Nishihama, R., Yamato, K. T. and Kohchi, T. Co-option of a photoperiodic growthphase transition system during land plant evolution, Nature Comm. 5, 3668 (2014). doi:
10.1038/ncomms4668
Website of the lab: http://www.plantmb.lif.kyoto-u.ac.jp/
Key words: land plant evolution, light signaling, plant development, Marchantia polymorpha6) Laboratory of Molecular and Cellular Biology of Totipotency -- From April 1, 2019 ~PI: NAKANO, Takeshi (Prof.) < tnakano@riken.jp>
Outline of the research
1. Plant chemical biology for molecular mechanism of plant growth based on cell regulation and photosynthesis.
2. Signaling network of brassinosteroid that cross talks with the other phytohomones and environmental condition.
3. Application of novel genes to regulate plant growth for useful crop production.
Publications
Nosaki, S., Miyakawa, T., Xu, Y., Nakamura, A., Hirabayashi, K., Asami, T., Nakano, T., Tanokura, M. Structural
basis for brassinosteroid response by BIL1/BZR1. Nature Plants, 4, 771-776 (2018). doi: 10.1038/s41477-018-0255-1.
Yamagami, A., Saito, C., Nakazawa, M., Fujioka, S., Uemura, T., Matsui, M., Sakuta, M., Osada, H., Nakano, A., Asami,T., Nakano, T. Evolutionarily conserved BIL4 interacts with the brassinosteroid receptor BRI1 and regulates cell
elongation. Scientific Reports 7(1) Article number 5739 (2017). doi: 10.1038/s41598-017-06016-2.
Taishi Nishimura , Ryo Nagao , Takumi Noguchi , Jon Nield , Fumihiko Sato, Kentaro Ifuku (2016) The N-terminal
sequence of the extrinsic PsbP protein modulates the redox potential of Cyt b559 in photosystem II. Scientific Reports
6, Article number: 21490 doi:10.1038/srep21490
Shimada, S., Komatsu, T., Yamagami, A., Nakazawa, M., Matsui, M., Kawaide, H., Natsume, M., Osada, H., Asami, T.,
Nakano, T. Formation and dissociation of BSS1 protein complex regulates plant development via brassinosteroid
signaling. Plant Cell. 27: 375-90. (2015). doi: 10.1105/tpc.114.131508.
Website of the lab: http://plantchembio.sun.bindcloud.jp/index.html
Key words: plant chemical biology, plant growth, phytohormone, brassinosteroid, photosynthesis.

7) Laboratory of Biosignals and Response
PI: NAGAO, Masaya (Prof.) <mnagao@kais.kyoto-u.ac.jp>
Outline of the research
1. Screening for discovery of bioactive natural products.
2. Elucidation of the cellular functions of zinc transporters, ZIPs, and ZnTs
Publications

14

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Fujimoto, S., Tsuji, T., Fujiwara, T., Takeda, T.A., Merriman, C., Fukunaka, A., Nishito, Y., Fu, D., Hoch, E., Sekler,
I., Fukue, K., Miyamae, Y., Masuda, S., Nagao, M., Kambe, T. The PP-motif in luminal loop 2 of ZnT transporters
plays a pivotal role in TNAP activation. Biochem J. 473 (17) 2611-2621 (2016). doi: 10.1042/BCJ20160324
Miyamae, Y., Nishito, Y., Nakai, N., Nagumo, Y., Usui, T., Masuda, S., Kambe, T., Nagao, M. Tetrandrine induces
lipid accumulation through blockade of autophagy in a hepatic stellate cell line. Biochem Biophys Res Commun.
477, 40-46 (2016). doi: 10.1016/j.bbrc.2016.06.018
Ohtera, A., Miyamae, Y., Yoshida, K., Maejima, K., Akita, T., Kakizuka, A., Irie, K., Masuda, S., Kambe, T.,
Nagao, M. Identification of a New Type of Covalent PPARγ Agonist using a Ligand-Linking Strategy. ACS Chem
Biol. 10, 2794-2804 (2015). doi: 10.1021/acschembio.5b00628
Hashimoto, A., Ohkura, K., Takahashi, M., Kizu, K., Narita, H., Enomoto, S., Miyamae, Y., Masuda, S., Nagao, M,
Irie, K., Ohigashi, H., Andrews, G.K., Kambe, T. Soybean extracts increase cell surface ZIP4 abundance and cellularzinc levels: a potential novel strategy to enhance zinc absorption by ZIP4 targeting. Biochem J. 472, 183193 (2015).
doi: 10.1042/BJ20150862
Ohtera, A., Miyamae, Y., Nakai, N., Kawachi, A., Kawada, K., Han, J., Isoda, H., Neffati, M., Akita, T., Maejima, K.,
Masuda, S., Kambe, T., Mori, N., Irie, K., Nagao, M. Identification of 6-octadecynoic acid from a methanol extractof Marrubium vulgare L. as a peroxisome proliferator-activated receptor γ agonist. Biochem Biophys Res Commun.
440, 204-209 (2013). doi: 10.1016/j.bbrc.2013.09.003
Website of the lab: http://www.seitaijoho.lif.kyoto-u.ac.jp/
Key words: bioactive compounds, screening, zinc, transporter

8) Laboratory of Applied Molecular Microbiology
PI: FUKUZAWA, Hideya (Prof.) < fukuzawa@lif.kyoto-u.ac.jp>
Outline of the research
We are focusing on the molecular bases of biological functions of photosynthetic microorganisms contributing to
production of food, carbon-neutral renewable bio-energy and industrial materials by revealing the molecularmechanisms of photosynthetic acclimation. Especially we employ a green alga, Chlamydomonas reinhardtii, as amodel eukaryotic microorganism using its genome information, mutants, and genetic/molecular/biochemical
techniques. The current projects are as follows: (1) Molecular characterization and modification of the carbonconcentrating mechanism supporting photosynthetic carbon fixation, bioenergy production, and cell proliferation, (2)Elucidation of regulatory network systems controlling photosynthesis by sensing changes in levels of supplied CO2
or nitrogen, (3) Molecular mechanisms of controlling of retrograde signal from chloroplast and sexual reproduction
by nutrient starvation.
Publications
Shinkawa H, et al.: Algal protein kinase, Triacylglycerol Accumulation Regulator 1, modulates cell viability andgametogenesis in carbon/nitrogen imbalanced conditions. Plant Cell Physiol. 60: 916–930 (2019)
Yamano T, Toyokawa C, Fukuzawa H*: High-resolution suborganellar localization of Ca2+-binding protein CAS, anovel regulator of CO2-concentrating mechanism. Protoplasma 255: 1015–1022 (2018) PMID: 29372336
Wang L, Yamano T,,, Fukuzawa H*: Chloroplast-mediated regulation of CO2-concentrating mechanism by Ca2+binding protein CAS in the green alga Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 113: 12586-12591(2016) PMID: 27791081
15

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Yamaoka Y, et al.: The bZIP1 transcription factor regulates lipid remodeling and contributes to ER stress managementin Chlamydomonas reinhardtii. Plant Cell 31: 1127–1140 (2019) PMID: 30894460
Nitta N, et al.: Intelligent Image-Activated Cell Sorting. Cell 175: 266–276 (2018) PMID: 30166209
Isozaki A, et al.: A practical guide to intelligent image-activated cell sorting. Nature Protocol. 14: 2370–2415 (2019).
PMID: 31278398
Website of the lab: http://www.molecule.lif.kyoto-u.ac.jp/
Key words: CO2-sensing mechanism, photosynthetic acclimation, retrograde signaling, autophagy, sexual
reproduction9) Laboratory of Molecular Biology of Bioresponse
PI: KATAYAMA, Takane (Prof.) <takane@lif.kyoto-u.ac.jp>
Outline of the research
Our aim is to decipher the molecular mechanism underlying the symbiotic relationship between gut microbes andhost, and to develop food-and health-oriented application research. We are also focused on the elucidation of
mechanisms of mRNA processing, export, and quality control in the nucleus in human and its industrial applications.
Publications
Sakanaka M, Hansen ME, Gotoh A, Katoh T, Yoshida K, Odamaki T, Yachi H, Sugiyama Y, Kurihara S, Hirose J,
Urashima T, Xiao JZ, Kitaoka M, Fukiya S, Yokota A, Lo Leggio L, Abou Hachem M, and Katayama T. Evolutionary
adaptation in fucosyllactose uptake systems supports bifidobacteria-infant symbiosis. Sci. Adv. 5:eaaw7696, (2019).
Gotoh A, Katoh T, Sakanaka M, Ling Y, Yamada C, Asakuma S, Urashima T, Tomabechi Y, Katayama-Ikegami A,
Kurihara S, Yamamoto K, Harata G, He F, Hirose J, Kitaoka M, Okuda S. and Katayama T. Sharing of human milkoligosaccharides degradants within bifidobacterial communities in faecal cultures supplemented with Bifidobacteriumbifidum. Sci. Rep. 8:13958. (2018).
Okamura M, Yamanaka Y, Shigemoto M, Kitadani Y, Kobayashi Y, Kambe T, Nagao M, Kobayashi I, Okumura
K, Masuda S. Depletion of mRNA export regulator DBP5/DDX19, GLE1 or IPPK that is a key enzyme for the
production of IP6, resulting in differentially altered cytoplasmic mRNA expression and specific cell defect. PLoS One,13, e0197165, (2018)
Yamada C, Gotoh A, Sakanaka M, Hattie M, Stubbs KA, Katayama-Ikegami A, Hirose J, Kurihara S, Arakawa T,
Kitaoka M, Okuda S, Katayama T, and Fushinobu S. Molecular insight into evolution of symbiosis between breastfed
infants and a member of the human gut microbiome Bifidobacterium longum. Cell Chem. Biol. 24:515-524. (2017).
Website of the lab: http://www.bunshioutou.lif.kyoto-u.ac.jp/index.html
Key words: gut microbes, symbiosis, mRNA, export

16

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 201910) Laboratory of Plant Developmental Biology
PI: ARAKI, Takashi (Prof.) <taraqui@lif.kyoto-u.ac.jp>
Outline of the research
We are interested in molecular mechanisms underlying plant’s responses to environment. Plants have evolved plastic
developmental programs with both genetic and epigenetic basis to adapt their sessile mode of life to changing
environment. Using an angiosperm, Arabidopsis thaliana and a liverwort, Marchantia polymorpha as model systems,
we have been investigating (1) regulation of growth phase transition (especially, flowering) in response toenvironmental signals, (2) long-distance systemic signaling in the control of development, (3) sexual reproduction
processes (especially, male gametogenesis and fertilization), and (4) origin and evolution of regulatory systems forplastic development.
Publications
Tuzuki, M., Futagami, K., Shimamura, M., Inoue, C., Kunimoto, K., Oogami, T., Tomita, Y., Inoue, K., Kohchi, T.,
Yamaoka, S., Araki, T., Hamada, T., and Watanabe, Y. An early arising role of microRNA156/529c-SPL module in
reproductive development revealed by the liverwort Marchantia polymorpha. Curr. Biol. 29: 3307-3314., e1-e5(2019). doi: 10.1016/ j.cub.2019.07.084
Hisanaga, T., Yamaoka, S., Kawashima, T., Higo, A., Nakajima, K., Araki, T., Kohchi, T., and Berger, F. Building new
insights in plant gametogenesis from an evolutionary perspective. Nature Plants 5: 663-669 (2019). doi:
10.1038/s41477-019-0466-0
Inoue, K., Nishihama, R., Araki, T., and Kohchi, T. Reproductive induction is far-red high irradiance response
mediated by phytochrome and PHYTOCHROME INTERACTING FACTOR in Marchantia polymorpha.
Plant Cell Physiol. 60: 1136-1145 (2019). doi: 10.1093/pcp/pcz029
Higo, A., Kawashima, T., Borg, M., Zhao, M., López-Vidriero, I., Sakayama, H., Montgomery, S. A., Sekimoto, H.,
Hackenberg, D., Shimamura, M., Nishiyama, T., Sakakibara, K., Tomita, Y., Togawa, T., Kunimoto, K., Osakabe, A.,
Suzuki, Y., Yamato, K. T., Ishizaki, K., Nishihama, R., Kohchi, T., Franco-Zorrilla, J. M., Twell, D., Berger, F., andAraki, T. Transcription factor DUO1 generated by neo-functionalization is associated with evolution of spermdifferentiation in plants. Nature Commun. 9(5283): 1-13 (2018). doi: 10.1038/s41467-018-07228-3
Endo, M., Yoshida, M., Sasaki, Y., Negishi, K., Horikawa, K., Daimon, Y., Kurotani, K.-i., Notaguchi, M., Abe, M., andAraki, T. Reevaluation of florigen transport kinetics with separation of function by mutations that uncouple flowering
initiation and long-distance transport. Plant Cell Physiol. 59: 1621-1629 (2018). doi: 10.1093/pcp/pcy063
Bowman, J.L., Kohchi, T., Yamato, K.T., Jenkins, J., Shu, S., Ishizaki, K., Yamaoka, S., Nishihama, R., Nakamura, Y.,
Berger, F., Adam, C., Aki, S.S., Althoff, F., Araki, T., [33 authors omitted] Inoue, K., [64 authors omitted] and Schmutz,
J. Insights into land plant evolution garnered from the Marchantia polymorpha genome. Cell 171: 287-304 (2017). doi:
10.1016/j.cell.2017.09.030
Higo, A., Niwa, M., Yamato, K. T., Yamada, L., Sawada, H., Sakamoto, T., Kurata, T., Shirakawa, M., Endo, M.,
Shigenobu, S., Ishizaki, K., Nishihama, R., Kohchi, T. and Araki, T. Transcriptional framework of male gametogenesis
in the liverwort Marchantia polymorpha L. Plant Cell Physiol. 57: 325-338 (2016). doi: 10.1093/pcp/pcw005
Website of the lab: http://www.plantdevbio.lif.kyoto-u.ac.jp/index.html
Key words: flowering, florigen, sexual reproduction, germ line specification, gametogenesis

17

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 201911) Laboratory of Plasma Membrane and Nuclear Signaling
PI: YOSHIMURA, Shigehiro (Associate Prof.) <yoshimura@lif.kyoto-u.ac.jp>
Outline of the research
Our laboratory studies dynamics of plasma membrane and cytoskeletal architectures by using a variety of techniquesin live-cell imaging, molecular and cellular biology, and bioinformatics. Our research interest covers a wide range of
biological problems from molecular to cellular levels. We try to elucidate the molecular mechanism underlying
structural dynamics of cellular architectures, as well as how a defect in such dynamics causes a disease. Specificresearch topics include: (1) how structural dynamics of actin network is regulated by related proteins and how afunctional defect of these proteins causes a disease, (2) how virus infection and endocytic process proceed bymembrane-bound proteins, cytoskeletal network and lipid membrane, and (3) how dynamic assemblydisassembly of
intracellular architectures (nuclear envelope, chromosome, etc) is regulated by mitotic phosphorylation.
Publications
Yoshida, A., Sakai, N., Uekusa, Y., Imaoka, Y., Itagaki, Y., Suzuki, Y., and Yoshimura, S.H. “Morphological changesof plasma membrane and protein assembly during clathrin-mediated endocytosis” PLOS Biol. 16(5): e2004786(2018). doi: 10.1371/journal.pbio.2004786.
Kumeta, M., Konishi, H.A., Zhang, W., Sakagami, S. and Yoshimura, S.H. “Prolines in the α-helix confer the
structural flexibility and functional integrity of importin β.” J. Cell Sci., 131(1): e0188764 (2018). doi:
10.1242/jcs.206326.
Konishi H.A., Asai S., Watanabe T. and Yoshimura S.H. “In vivo analysis of protein crowding within the nuclear porecomplex in interphase and mitosis” Sci. Rep., 7(1): 5709 (2017). doi: 10.1038/s41598-017-05959-w
Lolodi, O., Yamazaki, H., Otsuka, S., Kumeta, M. and Yoshimura S.H. “Dissecting in vivo steady-state dynamics ofkaryopherin-dependent nuclear transport.” Mol. Biol. Cell. 27: 167-176 (2016). doi: 10.1091/mbc.E15-08-0601
Yoshimura, S.H., Kumeta, M. and Takeyasu, K. “Structural mechanism of nuclear transport mediated by importin β
and flexible amphiphilic proteins.” Structure 22: 1699-1710 (2014). doi: 10.1016/j.str.2014.10.009
Website of the lab: http://www.chrom.lif.kyoto-u.ac.jp
Key words: atomic force microscopy, molecular crowding, cytoskeletal dynamics, membrane dynamics, mechanobiology, virus infection, bioinformatics

12) Laboratory of Developmental Neurobiology
PI: KENGAKU, Mineko (Prof.) < kengaku@icems.kyoto-u.ac.jp>
Outline of the research
We study the dynamics and mechanisms of the formation of neural networks in the brain. We also aim to develop liveimaging techniques for observation of molecular signals controlling cell motility in the developing brain.
Publications
Kawabata-Galbraith, K., Fujishima, K., Mizuno, H., Lee, S.J., Uemura, T., Sakimura, K., Mishina, M., Watanabe, N. andKengaku, M. MTSS1 regulation of actin-nucleating formin DAAM1 in dendritic filopodia determines final dendritic
configuration of Purkinje cells. Cell Rep. 24(1):95-106. (2018).doi: 10.1016/j.celrep.2018.06.013.
Wu, Y.K., Umeshima, H., Kurisu, J. and Kengaku, M. Nesprins and opposing microtubule motors generate a point force
driving directional nuclear motion in migrating neurons. Development. 2018 Mar 8; 145(5) pii: dev158782. (2018). doi:
10.1242/dev.158782.
18

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Fukumitsu, K., Fujishima, K., Yoshimura, A., Wu, Y.K., Heuser, J. and Kengaku, M. Synergistic action of dendritic
mitochondria and creatine kinase maintains ATP homeostasis and actin dynamics in growing neuronal dendrites. J.
Neurosci. 35(14):5707- 5723 (2015). doi: 10.1523/JNEUROSCI.4115-14.2015.
Fujishima, K., Horie, R., Mochizuki, A. and Kengaku, M. Principles of branch dynamics governing shape characteristics
of cerebellar Purkinje cell dendrites. Development 139: 3442-3455 (2012). doi: 10.1242/dev. 081315.
Website of the lab: http://www.kengaku.icems.kyoto-u.ac.jp/index.html
Key words: neuronal differentiation, dendrite, cell migration, cortex formation, neural circuit formation

13) Laboratory of Biochemical Cell Dynamics
PI: SUZUKI, Jun (Prof.) <jsuzuki@icems.kyoto-u.ac.jp>
Outline of the research
We are researching on biological phenomenon of our interests by unbiased screening-based identification of key
genes regulating it. Currently, we are interested in the phenomenon called phospholipid scrambling, which are
involved in variety of biological systems and human diseases. We can classify our research to 3 stages: to explore
new fields by identifying the key genes; to develop primary finding; to think how our finding is applicable to medicine
or biotechnology. Through all stages, we will conduct the interesting research and enjoy science.
Publication:
Suzuki, J., Imanishi, E. and Nagata, S. The Xkr8 phospholipid scrambling complex in apoptotic phosphatidylserine
exposure. Proc. Natl. Acad. Sci. USA 113: 9509-9514 (2016). doi: 10.1073/pnas.1610403113.
Suzuki, J., Imanishi, E. and Nagata, S. Exposure of phosphatidylserine by Xk-related protein family members. J. Biol.
Chem. 289: 30257-30267 (2014). doi: 10.1074/jbc.M114.583419.
Suzuki, J., Denning, D.P., Imanishi, E., Horvitz, H.R. and Nagata, S. Xk-related protein 8 and CED-8 promote
phosphatidylserine exposure in apoptotic cells. Science 341: 403-406 (2013). doi: 10.1126/science.1236758.
Suzuki, J., Fujii, T., Imao, T., Ishihara, K., Kuba, H. and Nagata, S. Calcium-dependent phospholipid scramblase
activity of TMEM16 protein family members. J. Biol. Chem. 288: 13305-13316 (2013). doi:
10.1074/jbc.M113.457937.
Suzuki, J., Sims, P.J., Umeda, M. and Nagata, S. Calcium-dependent phospholipid scrambling by TMEM16F. Nature,
468:834-838 (2010). doi: 10.1038/nature09583.
Website of the lab: http://www.suzuki.icems.kyoto-u.ac.jp
Key words: screening, gene identification, phospholipid scrambling, phagocytosis, medicine

14) Laboratory of Ultrastructural Virology
PI: NODA, Takeshi (Prof.) <t-noda@infront.kyoto-u.ac.jp>
Outline of the research
Virus infections are accompanied by numerous ultrastructural changes in viral and cellular components. Our laboratory
has been investigating the intracellular replication mechanism of influenza, Ebola and Lassa viruses by using virological,
molecular biological, and biochemical techniques combining with different microscopic methods such as electron
19

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
microscopy and high-speed atomic force microscopy. Visualization and characterization of the virus life cycle at thenano-mesoscopic level give us unique knowledge and novel paradigms, which will advance our understanding ofmolecular basis of the replication mechanism.
Publications
Sugita Y, Matsunami H, Kawaoka Y, Noda T, Wolf M. Cryo-EM structure of the Ebola virus nucleoprotein-RNA complex
at 3.6 Å resolution. Nature 563:137-140. (2018)
Noda, T., Murakami, S., Nakatsu, S., Imai, H., Muramoto, Y., Shindo, K., Sagara, H. and Kawaoka, Y. Importance ofthe 1+7 configuration of the ribonucleoprotein complexes for influenza A virus genome packaging. Nature
Communications 9:54 (2018).
Wan, W., Kolesnikova, L., Clarke, M., Koehler, A., Noda, T., Becker, S., and Briggs, J.A.G. Structure and assemblyof the Ebola virus nucleocapsid. Nature 551: 394-397 (2017).
Martyushev, A., Nakaoka, S., Sato, K., Noda, T. and Iwami, S. Modelling Ebola virus dynamics: Implications fortherapy. Antiviral Research 135: 62-73 (2016).
Nakatsu, S., Sagara, H., Sakai, Y. T., Sugaya, N., Noda, T. and Kawaoka, Y. Complete and incomplete genome
packaging of influenza A and B viruses. mBio 7: e01248-16 (2016).
Website of the lab: https://www.facebook.com/NodaLab/
Key words: Influenza virus, Ebola virus, Lassa virus

Division of Systemic Life Science
1) Laboratory of Single-Molecule Cell Biology
PI: WATANABE, Naoki (Prof.) <watanabe.naoki.4v@kyoto-u.ac.jp>
Outline of the research
By using high-resolution live-cell fluorescence Single-Molecule Speckle (SiMS) microscopy and our new multitarget
high-density labeling super resolution microscopy IRIS, we are trying to bridge the gap between molecular behavior
and cell/body functions including mechanotransduction, cancer invasion, tissue remodeling and drug response bydirect viewing of molecules in action.
Publications
Yamashiro, S., Taniguchi, D., Tanaka, S., Kiuchi, T., Vavylonis, D. and Watanabe N. Convection-induced biased
distribution of actin probes in live cells. Biophys. J. 116: 142-150 (2019). doi: 10.1016/j.bpj.2018.11.022
Mizuno, H., Tanaka, K., Yamashiro, S., Narita, A. and Watanabe, N. Helical rotation of diaphanous-related formin
mDia1 generates actin filaments resistant to cofilin. Proc. Natl. Acad. Sci. USA 115: E5000-E5007 (2018). doi:
10.1073/pnas.1803415115
Kiuchi, T., Higuchi, M., Takamura, A., Maruoka, M. and Watanabe, N. Multitarget super-resolution microscopy withhigh-density labeling by exchangeable probes. Nat. Methods 12: 743-746 (2015). doi: 10.1038/nmeth.3466
Higashida, C., Kiuchi, T., Akiba, Y., Mizuno, H., Maruoka, M., Narumiya, S., Mizuno, K. and Watanabe, N. F- andG-actin homeostasis regulates mechanosensitive actin nucleation by formins. Nat. Cell Biol. 15: 395-405 (2013). doi:
10.1038/ncb2693
20

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Mizuno, H., Higashida, C., Yuan, Y., Ishizaki, T., Narumiya, S. and Watanabe, N. Rotational movement of the formin
mDia1 along the double helical strand of an actin filament. Science 331: 80-83 (2011). doi:
10.1126/science.1197692
Website of the lab: http://www.pharm2.med.kyoto-u.ac.jp/2_index.html
Key words: single-molecule imaging, super-resolution microscopy, cancer therapy2) Laboratory of Molecular and Cellular Biology
PI: SAKAMAKI, Kazuhiro (Associate Prof.) <sakamaki.kazuhiro.7u@kyoto-u.ac.jp>
Outline of the research
We are interested in the signal transduction mechanisms underlying apoptotic cell death and the biologicalsignificance and physiological roles of cell death in organisms. To understand these issues, our main research focuseson the apoptosis executors, caspases, and is to visualize the functional processes of these molecules in cells using live
cell imaging and computer simulation. We are also trying to generate appropriate model animals such as mouse,
Xenopus, and medaka to control the phenomenon of apoptosis in organisms.
Publications
Jaspers, C., Fraune, S., Arnold, A.E., Miller, D.J., Bosch, T., Voolstra, C.R., and Consortium of Australian Academyof Science Boden Research Conference Participants. Resolving structure and function of metaorganisms through aholistic framework combining reductionist and integrative approaches. Zoology 133:81-87 (2019). doi:
10.1016/j.zool.2019.02.007.
Moya, A., Sakamaki, K., Mason, B.M., Huisman, L., Forêt, S., Weiss, Y., Bull, T.A., Tomii, K., Imai, K., Hayward,
D.C., Ball, E.E., and Miller, D.J. Functional conservation of the apoptotic machinery from coral to man: the diverseand complex Bcl-2 and caspase repertoires of Acropora millepora. BMC Genomics 17:62 (2016). doi:
10.1186/s12864-015-2355-x.
Sakamaki, K., Ishii, T.M., Sakata, T., Takemoto, K., Takagi, C., Takeuchi, A., Morishita, R., Takahashi, H., Nozawa,
A., Shinoda, H., Chiba, K., Sugimoto, H., Saito, A., Tamate, S., Satou, Y., Jung, S.-K., Matsuoka, S., Koyamada, K.,
Sawasaki, T., Nagai, T. and Ueno, N. Dysregulation of a potassium channel, THIK-1, targeted by caspase-8
accelerates cell shrinkage. Biochim. Biophys. Acta 1863: 2766-2783 (2016). doi: 10.1016/j.bbamcr.2016.08.010.
Sakamaki, K., Imai, K., Tomii, K. and Miller, D.J. Evolutionary analyses of caspase-8 and its paralogs: Deep originsof the apoptotic signaling pathways. BioEssays 37: 767-776 (2015). doi: 10.1002/bies.201500010.
Kominami, K., Nakabayashi, J., Nagai, T., Tsujimura, Y., Chiba, K., Kimura, H., Miyawaki, A., Sawasaki, T., Yokota,
H., Manabe, N. and Sakamaki, K. The molecular mechanism of apoptosis upon caspase-8 activation: quantitative
experimental validation of a mathematical model. Biochim. Biophys. Acta 1823: 1825–1840 (2012). doi:
10.1016/j.bbamcr.2012.07.003.
Website of the lab: http://www.mcb.lif.kyoto-u.ac.jp/
Key words: apoptosis, caspase, computer simulation, live imaging, optogenetics

21

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 20193) Laboratory of Immunobiology
PI: TAKAHARA, Kazuhiko (Associate Prof.) <ktakahar@zoo.zool.kyoto-u.ac.jp >Outline of the research
We focus on dendritic cells, macrophages, and their antigen receptor lectins that recognize polysaccharides on
pathogens. We are also interested in immunosuppressive mechanisms of pathogens. Based on these studies, we would
like to develop new methods to control immune system.
Publications
Ishiguro, T.*, Fukawa, T.*, Akaki, K., Nagaoka, K., Takeda, T., Iwakura, Y., Inaba, K., and Takahara, K. Absence of
DCIR1 reduces the mortality rate of endotoxemic hepatitis in mice. Eur. J. Immunol. 47, 704-712. (*equal
contribution) (2017). doi: 10.1002/eji.201646814
Taneo, J., Adachi, T, Yoshida, A., Takeyasu, K., Takahara, K.* and Inaba, K. Amyloid β oligomers induce interleukin1β production in primary microglia in a cathepsin B- and reactive oxygen species-dependent manner. Biochem.
Biophys. Res. Commun. 458, 561-567. (*corresponding author) (2015). doi: 10.1016/j.bbrc.2015.02.006
Tokieda, S., Komori, M., Ishiguro, Iwakura, Y., Takahara, K.* and Inaba, K. Dendritic cell immunoreceptor 1 alters
neutrophil responses in the development of experimental colitis. BMC Immunol. 16, 64. (*corresponding author)(2015). doi: 10.1186/s12865-015-0129-5
Adachi, T., Takahara, K., Taneo, J., Uchiyama, Y. and Inaba, K. Particle size of latex beads dictates IL-1β production
mechanism. Plos One 8, e68499. (2013). doi: 10.1371/journal.pone.0068499
Takahara, K., Arita, T., Tokieda, S., Shibata, N., Okawa, Y., Tateno, H., Hirabayashi, J. and Inaba, K. Difference infine specificity to polysaccharides of C. albicans mannoprotein between mouse SIGNR1 and human DC-SIGN.
Infect. Immun. 89, 1699-1706. (2012). doi: 10.1128/IAI.06308-11
Website of the lab: http://zoo.zool.kyoto-u.ac.jp/imm/
Key words: lectin, immune modulation, polysaccharide, disease models, dendritic cells4) Laboratory of Molecular Cell Biology and Development (Collaboration lab in RIKEN, Kobe)
PI (1): MATSUZAKI, Fumio (Prof.) <fumio.matsuzaki@riken.jp >Outline of the research
1. We investigate physical and molecular mechanisms, by which cell polarity and asymmetric division generate
cellular diversity.
2. We investigate genetic and epigenetic programs, by which the brain develops and maturates especially
focusing on the roles and behavior of neural stem cells. We use mouse as a simple mammalian brain model,
ferret as a complex mammalian brain model, and Drosophila as a genetic model system.
Publications
Suzuki, K.,#, Tsunekawa, Y.,# , Hernandez-Benitez, R.,#, Wu, J.,#, Zhu, J.,# et al. Matsuzaki, F., (28th/34 authors),
Belmonte, JC. In vivo genome editing via CRISPR-Cas9 mediated homology-independent targeted integration.
Nature 540,144–149 (2016). doi:10.1038/nature20565 #equal contribution

22

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Tsunekawa, Y.,#, Terhune, RK.,#, Fujita, I., Shitamukai, A., Suetsugu, T., and Matsuzaki F. Developing a de novo
targeted knock-in method based on in utero electroporation into the mammalian brain. Development 143, 3216-22(2016). doi: 10.1242/dev.136325 #equal contribution
Okamoto M, Miyata T, Konno D, Ueda HR, Kasukawa T, Hashimoto M, Matsuzaki F*, and Kawaguchi A*. Cell
cycle–independent transitions in temporal identity of mammalian neural progenitor cells. Nat Commun. 7:11349.
doi: 10.1038/ncomms11349. *corresponding authors. (2016).
Matsuzaki, F., and Shitamukai, A. Cell division modes and cleavage planes of neural progenitors during mammaliancortical development. Cold Spring Harb. Perspect. Biol. 7, (2015) a015719. doi:
10.1101/cshperspect.a015719.
Yoshiura, S., Ohta, N., and Matsuzaki, F. Tre1 GPCR signaling orients stem cell divisions in the Drosophila central
nervous system. Dev. Cell 22, 1-13 (2012). doi.org/10.1016/j.devcel.2011.10.027
Website of the lab: http://www.cdb.riken.jp/en/research/laboratory/matsuzaki.html
Key words: neural stem cells, brain development, mouse, ferret, Drosophila

PI (2): KITAJIMA, Tomoya (Associate Prof.) <tomoya.kitajima@riken.jp>
Outline of the research
We are interested in how chromosomes behave in time and space to archive correct chromosome segregation duringmeiosis and mitosis in mammalian oocytes and zygotes. Taking advantage of our live imaging technology, we conduct
comprehensive quantitative analysis of the chromosome dynamics.
Publications
Ding, Y., Kaido, M., Llano, E., Pendas, A.M., and Kitajima, T.S. The post-anaphase SUMO pathway ensures themaintenance of centromeric cohesion through meiosis I-II transition in mammalian oocytes. Current Biology 28(10),1661–1669 (2018). doi: 10.1016/j.cub.2018.04.019.
Kyogoku, H., & Kitajima, T. S. Large cytoplasm is linked to the error-prone nature of oocytes. Developmental Cell,
41(3), 287–298 (2017). doi:10.1016/j.devcel.2017.04.009.
Sakakibara, Y., Hashimoto, S., Nakaoka, H., Kouznetsova, A., Hӧӧg, C., and Kitajima, T.S. Bivalent separation into
univalents precedes age-related meiosis I errors in oocytes.Nature Communications, 6, 7550 (2015). doi:
10.1038/ncomms8550
Yoshida, S., Kaido, M., and Kitajima, T.S. Inherent instability of correct kinetochore-microtubule attachments duringmeiosis I in oocytes. Developmental Cell, 33, 589–602 (2015). doi: 10.1016/j.devcel.2015.04.020
Website of the lab: http://chromosegr.riken.jp/index_en.html
Key words: chromosome, meiosis, oocyte, zygote

PI (3): TAKASATO, Minoru (Associate Prof.) <minoru.takasato@riken.jp>
Outline of the research
Utilizing our unique technology that generates kidney organoids from human pluripotent stem cells, we are focusing
particularly on uncovering the developmental mechanisms of human mesoderm and the kidney. By precisely
23

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
recapitulating the developmental processes of human kidney in the directed differentiation of human pluripotent stem
cells, we are also aiming for the ultimate goal of generating a three-dimensional kidney that is functional and can betransplanted into patients.
Publications
Phipson, B., Er, P.X., Combes, A.N., Forbes, T.A., Howden, S.E., Zappia, L., Yen, H.-J., Lawlor, K.T.,
Hale, L.J., Sun, J., Wolvetang, E., Takasato, M., Oshlack, A., Little, M.H., Evaluation of variability
in human kidney organoids. Nat. Methods 16, 79–87 (2019). doi: 10.1038/s41592-018-0253-2
M. Takasato, P. X. Er, H. S. Chiu, M. H. Little, Generation of kidney organoids from human pluripotent stem cells.
Nat. Protoc. 11, 1681–1692 (2016). doi: 10.1038/nprot.2016.098
M. Takasato et al., Kidney organoids from human iPS cells contain multiple lineages and model human nephrogenesis.
Nature. 526, 564–8 (2015). doi: 10.1038/nature15695
M. Takasato, M. H. Little, The origin of the mammalian kidney: implications for recreating the kidney in vitro.
Development. 142, 1937–1947 (2015). doi: 10.1242/dev.104802
M. Takasato et al., Directing human embryonic stem cell differentiation towards a renal lineage generates aselforganizing kidney. Nat. Cell Biol. 16, 118–26 (2014). doi: 10.1038/ncb2894
Website of the lab: https://www.bdr.riken.jp/en/research/labs/takasato-m/index.html
Key words: kidney organoid, directed differentiation, pluripotent stem cell, human development

5) Laboratory of Molecular Neurobiology
PI: KATOH, Hironori (Associate Prof.) <hirokato@pharm.kyoto-u.ac.jp>
Outline of the research
We study the relationship between the regulation of metabolism and signal transduction in cancer cells, and aim toelucidate the mechanisms underlying cancer development and progression.
Publications
Hamaoka, Y., Negishi, M., Katoh, H. Tyrosine kinase activity of EphA2 promotes its S897 phosphorylation andglioblastoma cell proliferation. Biochem. Biophys. Res. Commun. 499, 920-926 (2018) . doi:
10.1016/j.bbrc.2018.04.020.
Goji, T., Takahara, K., Negishi, M., Katoh, H. Cystine uptake through the cystine/glutamate antiporter xCT triggers
glioblastoma cell death under glucose deprivation. J. Biol. Chem. 292, 19721-19732 (2017). doi:
10.1074/jbc.M117.814392.
Hamaoka, Y., Negishi, M., Katoh, H. EphA2 is a key effector of the MEK/ERK/RSK pathway regulating glioblastoma
cell proliferation. Cell. Signal. 28, 937-945 (2016). doi: 10.1016/j.cellsig.2016.04.009.
Okuyama, Y., Umeda, K., Negishi, M., Katoh, H. Tyrosine phosphorylation of SGEF regulates RhoG activity and cell
migration. PLoS One 11, e0159617 (2016). doi: 10.1371/journal.pone.0159617.
Website of the lab: http://www.negishi.lif.kyoto-u.ac.jp/j/toppu.html
Key words: cancer, signal transduction, transporter, receptor
24

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 20196) Laboratory of Genetics
PI: IGAKI, Tatsushi (Prof.) <igaki@lif.kyoto-u.ac.jp>
Outline of the research
Our research focuses on the molecular basis of cell-cell communication that governs tissue growth, homeostasis, andcancer. We take advantage of the powerful genetics of Drosophila.
Research subjects:
1. Mechanism of cell competition
2. Genetic basis of tissue growth regulation
3. Molecular basis of tumor progression and metastasis
Publications
Nagata, R., Nakamura, M., Sanaki, Y., and Igaki, T. Cell competition is driven by autophagy. Dev Cell 51: 99-112(2019)
Katsukawa, M., Ohsawa, S., Zhang, L., Yan, Y., and Igaki, T. Serpin facilitates tumor-suppressive cell competitionby blocking Toll-mediated Yki activation in Drosophila. Curr Biol 28: 1756-1767 (2018)
Yamamoto, M., Ohsawa, S., Kunimasa, K., and Igaki, T. The ligand Sas and its receptor PTP10D drive
tumorsuppressive cell competition. Nature 542: 246-250 (2017).
Vaughen, J. and Igaki, T. Slit-Robo repulsive signaling excludes tumorigenic cells from epithelia. Dev Cell 39: 683695 (2016)
Nakamura, M., Ohsawa, S. and Igaki, T. Mitochondrial defects trigger proliferation of neighbouring cells via asenescence-associated secretory phenotype in Drosophila. Nat Commun 5: 5264 (2014).
Ohsawa, S., Sato, Y., Enomoto, M., Nakamura, M., Betsumiya, A. and Igaki, T. Mitochondrial defect drives
nonautonomous tumor progression through Hippo signaling in Drosophila. Nature 490: 547-551 (2012).
Website of the lab: http://www.lif.kyoto-u.ac.jp/genetics/english/
Key words: cell-cell communication, cancer, development, cell competition, Drosophila

7) Laboratory of Functional Biology
PI: KAKIZUKA, Akira (Prof.) <kakizuka@lif.kyoto-u.ac.jp>
Outline of the research
Using animal models of human diseases, such as neurodegenerations, cancers, and obesity-related diseases, and using
metabolic imaging techniques, we aim to elucidate molecular bases of such diseases and develop new strategies tocure or prevent them.
Publications
Ide Y, Horie T, Saito N, Watanabe S, Otani C, Miyasaka Y, Kuwabara Y, Nishino T, Nakao T, Nishiga M, Nishi H,
Nakashima Y, Nakazeki F, Koyama S, Kimura M, Tsuji S, Rodriguez RR, Xu S, Yamasaki T, Watanabe T, Yamamoto
M, Yanagita M, Kimura T, Kakizuka A, Ono K. Cardioprotective Effects of VCP Modulator KUS121 in Murine andPorcine Models of Myocardial Infarction. JACC Basic Transl Sci. 28;4(6):701-714. (2019). doi:
10.1016/j.jacbts.2019.06.001.

25

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Sugiyama Y, Shudo T, Hosokawa S, Watanabe A, Nakano M, Kakizuka A. Emodin, as a mitochondrial uncoupler,
induces strong decreases in adenosine triphosphate (ATP) levels and proliferation of B16F10 cells, owing to their poor
glycolytic reserve. Genes Cells. 24(8):569-584. (2019). doi: 10.1111/gtc.12712.
Alfaqaan S, Yoshida T, Imamura H, Tsukano C, Takemoto Y, Kakizuka A. PPARα-Mediated Positive-Feedback Loop
Contributes to Cold Exposure Memory. Sci Rep. 14;9(1):4538. (2019). doi: 10.1038/s41598-019-40633-3.
Nakano M, Imamura H, Sasaoka N, Yamamoto M, Uemura N, Shudo T, Fuchigami T, Takahashi R, andKakizuka A. ATP Maintenance via Two Types of ATP Regulators Mitigates Pathological Phenotypes in Mouse
Models of Parkinson's Disease. EBioMedicine. 22:225-241 (2017). doi: 10.1016/j.ebiom.2017.07.024.
Yoshida T, Kakizuka A, Imamura H. BTeam, a novel BRET-based biosensor for the accurate quantification of ATP
concentration within living cells. Sci Rep. 7:44873 (2017). doi: 10.1038/srep44873.
Website of the lab: http://www.funcbiol.lif.kyoto-u.ac.jp/
Key words: drug development, neurodegenerative diseases, cancer, obesity, ATP, FRET biosensor

8) Laboratory of Chromosome Function and Inheritance
PI: CARLTON, Peter (Associate Prof.) <carlton.petermark.3v@kyoto-u.ac.jp>
Outline of the research
We study how genetic information is correctly maintained and passed on through cell divisions. Combining molecular
genetic approaches with advanced microscopy and quantitative imaging, we focus on mechanisms of chromosome
pairing, recombination, and segregation and recombination in meiosis in the nematode C. elegans.
Publications
Sato-Carlton, A., Nakamura-Tabuchi, C., Chartrand, S.K., Uchino, T., and Carlton, P.M. Phosphorylation of thesynaptonemal complex protein SYP-1 promotes meiotic chromosome segregation. J. Cell Biol. 217, 555–570. (2017).
doi: 10.1083/jcb.201707161
Kafer, G.R., X. Li, T. Horii, I. Suetake, S. Tajima, I. Hatada, and P.M. Carlton. 5-Hydroxymethylcytosine Marks Sites
of DNA Damage and Promotes Genome Stability. Cell Rep. 14:1283–1292. (2016). doi:10.1016/j.celrep.2016.01.035.
Sato-Carlton, A., X. Li, O. Crawley, S. Testori, E. Martinez-Perez, A. Sugimoto, and P.M. Carlton. Protein
phosphatase 4 promotes chromosome pairing and synapsis, and contributes to maintaining crossover competencewith increasing age. PLoS Genet. 10:e1004638. (2014). doi:10.1371/journal.pgen.1004638.
Mishima, Y., C.D. Jayasinghe, K. Lu, J. Otani, M. Shirakawa, T. Kawakami, H. Kimura, H. Hojo, P. Carlton, S.
Tajima, and I. Suetake. Nucleosome compaction facilitates HP1γ binding to methylated H3K9. Nucleic Acids Res.
43:10200–10212. (2015). doi:10.1093/nar/gkv841.
Kafer, G.R., P.M. Carlton, and S.A. Lehnert. The histone variant H2A.Z is dynamically expressed in the developing
mouse placenta and in differentiating trophoblast stem cells. Placenta. 36:1325–1328. (2015).
doi:10.1016/j.placenta.2015.08.018.
Schermelleh, L., P.M. Carlton, S. Haase, L. Shao, L. Winoto, P. Kner, B. Burke, C.M. Cardoso, D.A. Agard, M.G.
Gustafsson, H. Leonhardt, and J.W. Sedat. Subdiffraction Multicolor Imaging of the Nuclear Periphery with 3D
Structured Illumination Microscopy. Science. 320:1332–1336. (2008). doi:10.1126/science.1156947.
26

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Website of the lab: https://www.carltonlab.org/
Key words: DNA damage, meiosis, Chromosome segregation, C. elegans, super-resolution microscopy9) Laboratory of Bioimaging and Cell Signaling
PI: MATSUDA, Michiyuki (Prof.) < matsudam@lif.kyoto-u.ac.jp>
Outline of the research
The current aim of our research is to decipher the mechanism underlying cell-to-cell communication. For this purpose,
we are visualizing the activities of signaling molecules by using probes based on the principle of Förster resonanceenergy transfer (FRET). The FRET biosensors are extremely powerful to visualize the spatiotemporal regulation of signaltransduction networks within cells and to analyze the activities of individual cells within tissues. We are also developing
a series of optogenetic tools to activate molecules of interest within the tissues of live mice. Our laboratory is in chargeof the core facility of fluorescence live imaging of Kyoto University.
Publications
Kinjo, T., Terai, K., Horita, S., Nomura, N., Sumiyama, K., Togashi, K., Iwata, S., and Matsuda, M. FRET-assisted
photoactivation of flavoproteins for in vivo two-photon optogenetics. Nat Methods. 16, 1029-1036, (2019)
Muta, Y., Fujita, Y., Sumiyama, K., Sakurai, A., Taketo, M. M., Chiba, T., Seno, H., Aoki, K., Matsuda, M. & Imajo, M.
Composite regulation of ERK activity dynamics underlying tumour-specific traits in the intestine. Nat. Commun. 9,2174, (2018).
Konagaya, Y., Terai, K., Hirao, Y., Takakura, K., Imajo, M., Kamioka, Y., Sasaoka, N., Kakizuka, A., Sumiyama, K.,
Asano, T. & Matsuda, M. A Highly Sensitive FRET Biosensor for AMPK Exhibits Heterogeneous AMPK Responses
among Cells and Organs. Cell Rep. 21, 2628-2638, (2017).
Website of the lab: http://www.fret.lif.kyoto-u.ac.jp/e-phogemon/index.htm
Key words: multiphoton fluorescence microscopy, biosensors, optogenetics, transgenic mouse

10) Laboratory of Theoretical Biology
PI: HONDA, Naoki (Associate Prof.) < honda.naoki.4v@kyoto-u.ac.jp>
Outline of the research
Our laboratory aims to elucidate the theoretical logic of dynamic living systems. By developing and simulating
mathematical models, we are trying to understand mechanisms underlying phenomena in a bottom-up manner. We arealso utilizing machine learning to extract hidden rules of dynamic, complicated phenomena from experimental
quantitative data in a top-down manner. By means of these theoretical approaches, we are studying neuronal wiring in
the brain, emotional neural dynamics, noise-resistant embryonic development, mechano-chemical mechanisms ofcollective cell migration, cytoskeleton-based cellular morphogenesis, identification of intracellular information
processing, and animal behavioral strategies.
Publications
Honda N*, Akiyama R, Sari DWK, Ishii S, Bessho Y and Matsui T: Noise-resistant developmental reproducibility invertebrate somite formation. PLoS Computational Biology (in press, doi: 10.1371/journal.pcbi.1006579)

27

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Yamaguchi S, Honda N*, Ikeda M, Tsukada Y, Nakano S, Mori I and Ishii S: Identification of animal behavioral
strategies by inverse reinforcement learning. PLoS Computational Biology 14(5): e1006122 (2018)
Honda N*: Revisiting chemoaffinity theory: Chemotactic implementation of topographic axonal projection PLoS
Computational Biology 13(8), e1005702 (2017)
Li Y, Nakae K, Ishii S and Honda N*: Uncertainty-dependent extinction of fear memory in an amygdala-mPFC neuralcircuit model. PLoS Computational Biology 12(9), e1005099 (2016)
Yamao M, Honda N (Co-first), Kunida K, Aoki K, Matsuda M and Ishii S Distinct predictive performance of Rac1
and Cdc42 in cell migration. Scientific Reports 5, 17527 (2015)
Website of the lab: https://sites.google.com/view/theoretical-biology/
Key words: Mathematical model, Computer simulation, Machine learning, Data-driven modeling, Data analysis

11) Laboratory of Brain Development and Regeneration
PI: IMAYOSHI, Itaru (Prof.) <imayoshi.itaru.2n@kyoto-u.ac.jp>
Outline of the research
We aim to understand the cellular and molecular mechanism of the growth and fate-determination of neural stem cells
in the developing and adult mammalian brain. We are also interested in the functional significance of postnatal/adultneurogenesis on higher brain functions, such as spatial learning/memory and olfactory-related behaviors. Our lab has
expertise in the optical regulation of gene expression and neuronal activity, genetic manipulation of neuraldevelopment and plasticity, and long-term monitoring of neural circuit plasticity in vivo with the two-photon
microscope and brain endoscope.
Publications
Sueda, R., *Imayoshi, I. (equal contribution), Harima, Y., and *Kageyama, R. High Hes1 expression and resultant
Ascl1 suppression regulate quiescent versus active neural stem cells in the adult mouse brain. Genes Dev, 33, 511523 (2019).
Yamada, M., Suzuki, Y., Nagasaki, S., Okuno, H. and *Imayoshi, I. Light-inducible Tet-gene expression system inmammalian cells. Cell Reports, 25, 487-500 (2018)*Suzuki, Y. and *Imayoshi, I. Network analysis of exploratory behaviors of mice in a spatial learning and memorytask. PLoS One Jul 10;12(7):e0180789 (2017). doi: 10.1371/journal.pone.0180789.
*Imayoshi, I. and *Kageyama, R. bHLH Factors in Self-Renewal, Multipotency, and Fate Choice of Neural
Progenitor Cells. Neuron 82: 9-23 (2014).
Sakamoto, M., Ieki, N., Miyoshi, G., Mochimaru, D., Miyachi, H., Imura, T., Yamaguchi, M., Fishell, G., Mori, K.,
Kageyama, R. and *Imayoshi, I. Continuous postnatal neurogenesis contributes to formation of the olfactory bulb
neural circuits and flexible olfactory associative learning. The Journal of Neuroscience 34: 5788-5799 (2014).
I*mayoshi, I., Isomura, A. (equal contribution), Harima, Y., Kawaguchi, K., Kori, H., Miyachi, H., Fujiwara, T.K.,
Ishidate, F. and *Kageyama, R. Oscillatory control of factors determining multipotency and fate in mouse neuralprogenitors. Science 342: 1203-1208 (2013).

28

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Imayoshi, I., Sakamoto, M., Ohtsuka, T., Takao, K., Miyakawa, T., Yamaguchi, M., Mori, K., Ikeda,
T., Itohara, S. and *Kageyama, R. Roles of continuous neurogenesis in the structural and functional
integrity of the adult forebrain. Nature Neuroscience 11: 1153-1161 (2008).
Website of the lab: https://brainnetworks.jimdofree.com
Key words: Neural stem cells, Neurogenesis, Optogenetics, Hippocampus, Olfactory bulb

12) Laboratory of Genome Maintenance
PI: MATSUMOTO, Tomohiro (Prof.) <tmatsumo@house.rbc.kyoto-u.ac.jp>
Outline of the research
The spindle checkpoint is a unique negative feedback that converts/amplifies a physical signal sensed by kinetochores(attachment of the spindle and/or tension), and regulates the timing of sister chromatid separation for equal
chromosome segregation. Mad2, a signal carrier of this feedback, plays a vital role in the spindle checkpoint.
It is specifically localized at unattached kinetochores that are the origin of the checkpoint signal. Mad2 targets CDC20
and inhibits its activity to promote sister chromatid separation. We study Mad2, a central player of the spindle
checkpoint, to reveal mechanisms which regulate the activity of Mad2.
Publications
Kitagawa T., Ishii K., Takeda K. and Matsumoto T. The 19S proteasome subunit Rpt3 regulates distribution of CENPA by associating with centromeric chromatin. Nat Commun. (2014). doi: 10.1038/ncomms4597.
Horikoshi Y, Habu T and Matsumoto T. An E2 enzyme Ubc11 is required for ubiquitination of Slp1/Cdc20 andspindle checkpoint silencing in fission yeast. Cell Cycle. 12:961-71 (2013).
Ito D, Saito Y and Matsumoto T. Centromere-tethered Mps1 pombe homolog (Mph1) kinase is a sufficient marker
for recruitment of the spindle checkpoint protein Bub1, but not Mad1. Proc Natl Acad Sci U S A. 109:209-14 (2012).
Website of the lab: http://house.rbc.kyoto-u.ac.jp/radiation_system/
Key words: chromosome, mitosis, centromere

13) Laboratory of Genome Damage Signaling
PI: TAKATA, Minoru (Prof.) < mtakata@house.rbc.kyoto-u.ac.jp>
Outline of the research
DNA damage response (DDR) is the fundamental mechanism that stabilizes our genome. Genome stability underlies
all biological processes. We try to identify molecules involved in genome stability/replication stress/DDR by methods
such as screening mutations in human patients, and further analyze their function using genome engineering in various
cell lines, iPS cells, and model organisms.
Publications
Minako Mori, Asuka Hira, Kenichi Yoshida, Hideki Muramatsu, Yusuke Okuno, Yuichi Shiraishi, Michiko Anmae,
Jun Yasuda, Shu Tadaka, Kengo Kinoshita, Tomoo Osumi, Yasushi Noguchi, Souichi Adachi, Ryoji Kobayashi,
Hiroshi Kawabata, Kohsuke Imai, Tomohiro Morio, Kazuo Tamura, Akifumi Takaori-Kondo, Masayuki Yamamoto,
Satoru Miyano, Seiji Kojima, Etsuro Ito, Seishi Ogawa, Keitaro Matsuo, Hiromasa Yabe, Miharu Yabe, Minoru
Takata. Pathogenic mutations identified by a multimodality approach in 117 Japanese Fanconi anemia patients.
29

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Haematologica 2019 Oct;104(10):1962-1973.
Replication stress induces accumulation of FANCD2 at central region of large fragile genes. Yusuke Okamoto,
Watal M. Iwasaki, Kazuto Kugou, Kazuki K. Takahashi, Arisa Oda, Koichi Sato, Wataru Kobayashi, Hidehiko
Kawai, Ryo Sakasai, Akifumi Takaori-Kondo, Takashi Yamamoto, Masato T. Kanemaki, Masato Taoka, Toshiaki
Isobe, Hitoshi Kurumizaka, Hideki Innan, Kunihiro Ohta, Masamichi Ishiai1, Minoru Takata．Nucleic Acid Res.
2018 Apr 6;46(6):2932-2944. doi: 10.1093/nar/gky058.
Inano, S., Sato, K., Katsuki, Y., Kobayashi, W., Tanaka, H., Nakajima, K., Nakada, S., Miyoshi, H., Knies, K.,
Takaori-Kondo, A., Schindler, D., Ishiai, M., Kurumizaka, H., Takata, M. RFWD3-mediated ubiquitination promotes
timely removal of both RPA and RAD51 from DNA damage sites to facilitate homologous recombination. Mol Cell.
66 (5):622-634.e8. (2017). doi: 10.1016/j.molcel.2017.04.022. PMID: 28575658
Knies, K., Inano, S., Ramírez, M. J., Ishiai, M., Surallés, J., Takata, M., and Schindler, D. Biallelic mutations in theubiquitin ligase RFWD3 cause Fanconi anemia. Journal of Clinical Investigation (2017). 127 (8):3013-3027. doi:
10.1172/JCI92069. Epub 2017 Jul 10. PMID: 28691929
Katsuki, Y. and Takata, M. Defects in HR repair behind the human diseases: FA and HBOC. Endocr. Relat. Cancer(2016). PMID: 27550963
Hira, A., Yoshida, K., Sato, K., Okuno, Y., Shiraishi, Y., Chiba, K., Tanaka, H., Miyano, S., Shimamoto, A., Tahara,
H., Ito, E., Kojima, S., Kurumizaka, H., Ogawa, S., Takata, M., Yabe, H. and Yabe, M. Mutations in the gene encoding
the E2 conjugating enzyme UBE2T cause fanconi anemia. Am. J. Hum. Genet. 96: 1001-1007 (2015). doi:
10.1016/j.ajhg.2015.04.022. PMID: 26046368
Unno, J., Itaya, A., Taoka, M., Sato, K., Tomida, J., Sakai, W., Sugasawa, K., Ishiai, M., Ikura, T., Isobe, T.,
Kurumizaka, H. and Takata, M. FANCD2 binds CtIP and regulates DNA-end resection during DNA interstrand
crosslink repair. Cell Rep. 7:1039-47 (2014). doi: 10.1016/j.celrep.2014.04.005
Website of the lab: http://house.rbc.kyoto-u.ac.jp/late-effect
Key words: DNA damage response, DNA repair, genetic disorders, genome editing, Fanconi anemia

14) Laboratory of Cancer Cell Biology
PI: HARADA, Hiroshi (Prof.) < harada.hiroshi.5e@kyoto-u.ac.jp>
Outline of the research
Cells maintain their functions and morphology by exploiting a suitable adaptive response system to diverse andcomplex tissue microenvironments. Several lines of evidence have suggested that hypoxic, acidic and nutrientdepleted microenvironments exist in solid tumors and induce malignant phenotypes and chemo/radioresistance ofcancer cells. We aim to elucidate molecular mechanisms underlying both cellular adaptive responses to the tumorspecific microenvironments and malignant progression of cancer cells.
Publications:
Goto, Y., Zeng, L., Yeom, C. J., Zhu, Y., Morinibu, A., Shinomiya, K., Kobayashi, M., Hirota, K., Itasaka, S.,
Yoshimura, M., Tanimoto, K., Torii, M., Sowa, T., Menju, T., Sonobe, M., Kakeya, H., Toi, M., Date, H., Hammond
E. M, Hiraoka, M. and Harada, H. UCHL1 provides diagnostic and antimetastatic strategies due to its deubiquitinating
effect on HIF-1α. Nature Commun. 6: 6153 (2015). doi: 10.1038/ncomms7153

30

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Zeng, L., Morinibu, A., Kobayashi, M., Zhu, Y., Wang, X., Goto, Y., Yeom, C. J., Zhao, T., Hirota, K., Shinomiya,K., Itasaka, S., Yoshimura, M., Guo, G., Hammond, E. M., Hiraoka, M. and Harada, H. Aberrant IDH3alphaexpression promotes malignant tumor growth by inducing HIF-1-mediated metabolic reprogramming andangiogenesis. Oncogene 34: 4758-4766. (2015). doi: 10.1038/onc.2014.411
Harada, H., Inoue, M., Itasaka, S., Hirota, K., Morinibu, A., Shinomiya, K., Zeng, L., Ou, G., Zhu, Y., Yoshimura,M., McKenna, W. G,, Muschel, R. J. and Hiraoka, M. Cancer cells that survive radiation therapy acquire HIF-1
activity and translocate towards tumour blood vessels. Nature Commun. 3: 783 (2012). doi:10.1038/ncomms3314.
Website of the lab: http://www.rbc.kyoto-u.ac.jp/cancer_biology/
Key words: cancer, tumor microenvironments, hypoxia, chemo/radioresistance15) Laboratory of Laboratory of Chromatin Regulatory Network
PI: IKURA, Tsuyoshi (Associate Prof.) <ikurat@house.rbc.kyoto-u.ac.jp>
Outline of the research
The eukaryotic genome is tightly packed into the chromatin, a hierarchically organized complex of DNA, histone andnonhistone proteins. This packing represents a common obstacle for the metabolic processes of DNA includingtranscription, replication, recombination, and DNA repair. Current evidence indicates that chromatin reorganization
involving histone modification, histone variant exchange, histone eviction and ATP-dependent chromatin remodelingplay an integral role in DNA repair and DNA damage response. However, it remains unclear how such chromatin
reorganization is coupled with the initiation of DNA repair process and/or activation of checkpoint machinery after
DNA damage. We are now investigating the following issues:
1.The molecular mechanisms by which the TIP60 histone acetylase complex regulates histone H2AX exchange
induced by ionizing radiation.
2.The cross-talk between the histone signaling network regulated by histone H2AX exchange and DNA damage
response pathways.
Publications
Ikura, M., Furuya, K., Fukuto, A., Matsuda, R., Adachi, J., Matsuda, T., Kakizuka A., Ikura, T. Coordinated regulationof TIP60 and PARP-1 in damaged chromatin dynamics. Mol Cell Biol. 36:1595-1607 (2016). doi:
10.1128/MCB.01085-15.
Ikura, M., Furuya, K., Matsuda, S., Matsuda, R., Shima, H., Adachi, J., Matsuda, T., Shiraki, T., Ikura, T. Acetylationof histone H2AX at Lys 5 by the TIP60 histone acetyltransferase complex is essential for the dynamic binding of
NBS1 to damaged chromatin. Mol Cell Biol. 35: 4147-4157 (2015). doi: 10.1128/MCB.00757-15.
Ikura T., Tashiro, S., Kakino, A., Shima, H., Jacob, N., Amunugama, R., Yoder, K., Izumi, S., Kuraoka, I., Tanaka,K., Kimura, H., Ikura, M., Nishikubo, S., Ito, T., Muto, A., Miyagawa, K., Takeda, S., Fishel, R., Igarashi, K., *Kamiya,
K. DNA damage-dependent acetylation and ubiquitination of H2AX enhances chromatin dynamics. Mol Cell Biol.
27:7028-7040 (2007). doi:10.1128/MCB.00579-07
Ikura, T., Ogryzko, V V., Grigoriev, M., Groisman, R., Wang, J., Horikoshi, M., Scully, R., Qin, J., Nakatani, Y
Involvement of the TIP60 Histone Acetylase Complex in DNA repair and apoptosis. Cell. 102:463-473 (2000).
doi.org/10.1016/S0092-8674(00)00051-9
Website of the lab: http://house.rbc.kyoto-u.ac.jp/mutagenesis2/index1
Key words: chromatin dynamics, histone acetyltransferase, histone variant, DNA damage response31

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 201916) Laboratory of RNA Viruses
PI: TOMONAGA, Keizo (Prof.) <tomonaga@infront.kyoto-u.ac.jp>
Outline of the research
The main purpose of our research is to investigate the molecular mechanisms underlying the replication andpathogenesis of animal-derived RNA viruses. Analysis of the endogenization of RNA viruses and its role on hostvirus
co-evolution is also focused on this laboratory.
Publications
Ikeda, Y., Makino, A., Holditch, S. J., Lu, B., Dietz, A. B. and Tomonaga, K. A novel intranuclear RNA vector system
for long-term stem cell modification. Gene Ther. 23: 256-262 (2016). doi: 10.1038/gt.2015.108
Matsumoto, Y., Hayashi, Y., Omori, H., Honda, T., Daito, T., Horie, M., Ikuta, K., Fujino, K., Nakamura, S., Schneider,
U., Chase, J., Yoshimori, T., Schwemmle, M. and Tomonaga, K. Bornavirus closely associates and segregates withhost chromosomes to ensure persistent intranuclear infection. Cell Host Microbe 11:492-503 (2012). doi:
10.1016/j.chom.2012.04.009
Horie, M., Honda, T., Suzuki, Y., Kobayashi, Y., Daito, T., Oshida, T., Ikuta, K., Jern, P., Gojobori T., Coffin, J. M.
and Tomonaga, K. Endogenous non-retroviral RNA virus elements in mammalian genomes. Nature 463:84-87 (2010).
doi: 10.1038/nature08695
Website of the lab: https://t.rnavirus.virus.kyoto-u.ac.jp/
Key words: bornavirus, endogenous viruses, RNA virus vector

17) Laboratory of Cell Division and Differentiation
PI: TOYOSHIMA, Fumiko (Prof.) <ftoyoshi@infront.kyoto-u.ac.jp>
Outline of the research
Balance between self-renewal and differentiation of stem cells is essential for tissue homeostasis. Biased stem cell
self-renewal or differentiation leads to changes in tissue organization. Our group studies on the mechanisms ofsymmetric/asymmetric stem cell division, stem cell differentiation, stem cell plasticity, and cell lineage-commitment
in tissue homeostasis and regeneration. We are interested in how tissue stem cells adapt to physiological changes ofthe body throughout life stages, such as pregnancy, obesity and aging.
Publications
Ichijo, R., Kobayashi, H., Yoneda, S., Iizuka, Y., Kubo, H., Matsumura, S., Kitano, S., Miyachi, H., Honda, T., andToyoshima, F. Tbx3-dependent amplifying stem cell progeny drives interfollicular epidermal expansion during
pregnancy and regeneration. Nat. Commun. 8: 508 (2017). doi:10.1038/s41467-017-00433-7
Matsumura, S., Kojidani, T., Kamioka, Y., Uchida, S., Haraguchi, T., Kimura, A., and Toyoshima, F. Interphaseadhesion geometry is transmitted to an internal regulator for spindle orientation via caveolin-1. Nat. Commun.
7:11857 (2016). doi: 10.1038/ncomms11858
Iwano, S., Satou, A., Matsumura, S., Sugiyama, N., Ishihama, Y., and Toyoshima, F. PCTK1 regulates
integrindependent spindle orientation via PKA regulatory subunit KAP0 and myosin X. Mol. Cell. Biol. 35, 11971208(2015).

32

Global Frontier in Life Science
Graduate School of Biostudies (GSB), Kyoto University

Research Fields and Contents of Research – as of December, 2019
Matsumura S., Hamasaki M., Yamamoto T., Ebisuya M., Sato M., Nishida E. and Toyoshima F. ABL1 regulates
spindle orientation in adherent cells and mammalian skin. Nat. Commun. 3:626 (2012). doi: 10.1038/ncomms 1634
Website of the lab: https://www2.infront.kyoto-u.ac.jp/Toyoshima-HP/index-En.html
Key words: oriented cell division, stem cells, tissue homeostasis18) Laboratory of Cellular and Molecular Biomechanics
PI: ADACHI, Taiji (Prof.) <adachi@infront.kyoto-u.ac.jp>
Outline of the research
We aim to clarify the mechanisms by which cells sense mechanical stimuli and regulate their activities in tissue
adaptation, regeneration and stem cell differentiation in morphogenesis. Based on multiscale biomechanics, our groupis involved in the integrated biomechanics and mechanobiology researches of modeling and simulation combinedwith experiments, focusing on mechano-biochemical couplings in the system dynamics.
Publications
Takeda, H., Kameo, Y., Inoue, Y., Adachi, T. An energy landscape approach to understanding variety and robustness
in tissue morphogenesis. Biomech Model Mechanobiol. (2019). doi: 10.1007/s10237-019-01222-5
Ando, Y., Okeyo, K. O., Adachi, T. Modulation of adhesion microenvironment using mesh substrates triggers selforganization and primordial germ cell-like differentiation in mouse ES cells. APL Bioeng, 3: 016102 (2019). doi:
10.1063/1.5072761
Maki, K., Han, S. W., Hirano, Y., Yonemura, S., Hakoshima, T., Adachi, T. Real-time TIRF observation of vinculin
recruitment to stretched α-catenin by AFM. Sci Rep, 8: 1575 (2018). doi: 10.1038/s41598-018-20115-8
Okuda S., Takata, N., Hasegawa, Y., Kawada, M., Inoue, Y., Adachi, T., Sasai, Y., Eiraku, M. Strain-triggeredmechanical feedback in self-organizing optic cup morphogenesis. Sci. Adv. 4-11: eaau1354 (2018). doi:
10.1126/sciadv.aau1354
Kim, Y. K., Kameo, Y., Tanaka, S. and Adachi, T. Capturing microscopic features of bone remodeling into amacroscopic model based on biological rationales of bone adaptation. Biomech. Model Mechanobiol. 16-5:
16971708 (2017). doi: 10.1007/s10237-017-0914-6
Website of the lab: https://www2.infront.kyoto-u.ac.jp/bf05/index-e.html
Key words: biomechanics, mechanobiology, adaptation, morphogenesis, modeling and simulation

33