Department of Biological Sciences

Department of
Biological Sciences

Department of
Biological Sciences

The Department of Biological Sciences, Graduate
School of Science, offers a variety of graduate
programs including lectures on a wide range of current
biology, research training and advanced seminars
focusing on specific topics. The programs are guided
by researchers at the Department of Biological
Sciences, Institute for Protein Research, Institute of
Scientific and Industrial Research, Research Instituteof Microbial Diseases, Genome Information ResearchCenter, Frontier Biosciences, and three affiliatedinstitutes outside the university.

For detailed information of research topics, see thefollowing pages and http://www.bio.sci.osakau.ac.jp/en

The Department of Biological Sciences, Graduate
School of Science, was reorganized in 1996 by
combining two departments, Physiology andBiochemistry, both of which had been founded in 1953.
As a result of reorganization and together with thecooperation of three institutes outside the university,
the research conducted at the department covers a wide
range of the research fields of current biology and life
sciences, which have been rapidly expanding.
When the Department of Biology for undergraduate
studies started with three laboratories in 1949, two ofthem were protein chemistry (Professors Akabori andOkunuki) and one for biophysical cell biology(Professor Kamiya). The department was different
from other biology, zoology and/or botany departments
at that time. We follow this unique tradition in amodernized way and are always aiming at developing
newresearch fields in biology, especially in"supramolecular biology" which might surpass
ordinary molecular biology and ultimately elucidate
the life and living organisms at the atomic andsupramolecular levels. To pursue this task, wewelcome students who have backgrounds other thanbiology, such as chemistry and physics. Of course, we
also welcome students with a solid background in
biology. New research fields will be established in thiskind of amalgamating atmosphere.
Postgraduate students enrolled in the Master and/orDoctoral programs are requested to conduct their own
researches in the laboratories to be conferred with theirdegrees. The research is supervised by one of thesupervisors of the Graduate School. In the doctor
course, two advisors in addition to the supervisor will
guide your research.

Home Page
https://www.bio.sci.osaka-u.ac.jp

Graduate School of Science
2023-2024

Department of Biological Sciences

Laboratory of Cellular & Structural Biology
Members

Takahide KON (Professor), Ryosuke YAMAMOTO (Assistant Professor),
Hiroshi IMAI (Assistant Professor)

TEL・FAX

06-6850-5435

Home Page

http://www.bio.sci.osaka-u.ac.jp/bio_web/lab_page/kon/[Research interests]
In the cells that make up our bodies, a wide variety ofmacromolecules including proteins move quickly at the velocity ofseveral meters per second using thermal energy. However, that is
not useful for the long-distance transportation to the specificdirection in the cells because the direction of the thermal motion is
random. For example, in an elongated neuron with the length of 1m, it will take more than 100 years to transport an average-sized
protein from the cell body to the nerve terminal by the thermal
motion. Eukaryotic cells manage this problem by establishing
intracellular transport systems that powers a wide variety offundamental biological processes including ciliary beating, cell
division, cell migration and active transport of numerous cargoes.

e-mailtakahide.kon@bio.sci.

analysis. Recently, we havefocused on a huge motor protein
complex, dynein, which is theheart of the transport system
toward the center of the cells,
and determined its atomic
structures. We have also started
research projects to achieve acomprehensive understanding ofmRNA transport systems inneurons.

The partial loss of the function has been implicated inneurodegenerative disease, infertility and developmental
abnormality. Our laboratory aims to elucidate the molecularmechanism underlying the intracellular transport system by means

Upper panel: Atomic structure of “Dynein”,
the heart of the transport system.
Lower panel: Single-molecule observation of dynein
moving along a microtubule track.

of atomic-level structural analysis and single-molecule functional

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Laboratory of Single Molecule Biology
Members

Masahiro UEDA(Professor), Takayuki Ariga (Associate Professor)
Satomi MATSUOKA (Assistant Professor)

TEL・FAX

Tel: 81-6-6879-4611/・Fax: 81-6-6879-4613

Home Page

http://www.fbs.osaka-u.ac.jp/eng/general/lab/022/

e-mailmasahiroueda@fbs.

［Research projects］［Research interests］
Living cells are complex but well-organized systems comprisingvarious kinds of biomolecules. Because biomolecules operatestochastically under the strong influence of thermal fluctuations,living cells can be referred to as stochastically-operating
biomolecular computation systems. Through the dynamic
processes in reaction networks of biomolecules, cells can
respond flexibly and adaptively to environmental changes.
Recent progress in single molecule imaging techniques has madeit possible to monitor directly the stochastic behaviors of
biomolecules in living cells, in which the locations, movements,
turnovers, and complex formations of biomolecules can bedetected quantitatively at the single molecule level, providing
powerful tools to elucidate molecular mechanisms of
intracellular signaling processes. Our laboratory develops
quantitative single-molecule imaging methods, computationalmodeling methods and biochemical synthetic methods to reveal
the molecular mechanisms of cellular chemotaxis with singlemolecule resolution.

1)
2)
3)

Development of automated in-cell single-molecule imaging
system (AISIS)
Single-molecule biology of chemotactic signaling system
Functional roles of non-thermal fluctuations in living cells

Left: Chemotaxis of Dictyostelium discoideum amoebae to cyclic
AMP gradients.
Middle: Total internal reflection fluorescence microscopy(TIRFM) for single molecule imaging.
Right: Single molecule imaging of PTEN molecules on themembrane of living cells. Individual white spots represent single
molecules of PTEN.

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Genome Structure andFunction
Members

Chikashi OBUSE (Professor), Koji NAGAO (Associate Professor), Shin-Ya ISOBE (Assistant Professor)

TEL・FAXTel : 06-6850-5812

Home Page

http://www.bio.sci.osaka-u.ac.jp/bio_web/lab_page/obuse/［Research Interest］
Molecular mechanism for genetic and epigenetic
inheritances in mammalian cells
The ability of cells to store, retrieve, and translate thegenetic information is essential for making andmaintaining living organisms. The genetic information of
mammalian cells is preserved in the nucleus, in which
DNA together with proteins and RNA form a complex
called chromatin. Different types of cells in our body are
originated from a one cell embryo. Thus, such different
types of cells still possess same genetic information, but
their cellular identities are determined by each cell-type
specific gene expression.
This cell-type specific gene
expression is controlled by
epigenetic
information
including DNA methylation,
histonepost-translational
modifications and chromatin
structure. These epigenetic
information or epigenomes

e-mailobuse@bio.sci.

can be changed during differentiation or byenvironmental factors, but are also maintained andinherited by the next generation if cellular identity isfixed. We are interested in genetic and epigenetic
mechanisms to inherit the genetic information andutilize it properly. In addition, we want to understandhow cell-type specific epigenome can be switched or
maintained through cell division at molecular level. We
employ omics approaches using mass spectrometry andnext generation sequencer, as well as molecularbiological and genetical, biochemical, and cellbiological approaches, to elucidate these issues.

Mass spectrometer for proteomic analysis

Next generation sequencer for genomics

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Laboratory of Plant Development
Members

Tatsuo KAKIMOTO (Professor), Shinobu TAKADA (Assistant Professor),
Pingping QIAN (Assistant professor) ,Yuki SAKAMOTO (Assistant professor)

TEL・FAX

06-6850-5421

Home Page

https://kakimoto0.wixsite.com/kakimoto-lab［Research interests］

Plant development relies on coordinated division,differentiation and expansion of cells. In order to understandthe underlying mechanisms, we study both inter-cellularcommunication and cellular events. Plant hormones play
pivotal roles in almost all processes of plant development.
We have identified biosynthetic enzymes and receptors ofcytokinins, and clarified the role of cytokinins in plantdevelopment. We are also working on the roles of secretory
signaling peptides. We identified several peptides that
regulate plant development, including EPF1, which regulatespacing of stomata; EPF2 and stomagen, which regulate
epidermal cell number, CLE9/10 peptide that regulates
stomatal number and vascular cell pattern; and CLE25,26,45,
which regulate phloem formation. We are also working ontranscription factors that regulate the development of
epidermis, vascular cells, and pericycle. We would like tounderstand regulatory networks, consisting of transcription
factors and intercellular signaling molecules, that regulate
plant development.

e-mailkakimoto@bio.sci

We are also trying to elucidate the molecular mechanisms that
regulate the morphology and dynamics of organelles by using
fluorescence and luminescence imaging and proteomic
analysis.

Left, cross section of a lateral root showing expression of
PFA (magenta) in the xylem-pole pericycle. PFA/PFB
transcription factor complex confer the competence of
pericycle to undergo auxin-induced cell division andlateral root primordial formation. Right, PFA/PFB
regulates target genes conferring the pericycle identity.

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Cell Biology
Members

Kenji MATSUNO (Professor), Mikiko INAKI (Associate Professor),
Daiki UMETSU (Associate Professor ）TEL・FAX

06-6850-5804/5805

Home Page

http://www.bio.sci.osaka-u.ac.jp/bio_web/lab_page/matsuno/Etop.html

e-mailkmatsuno@bio.sci.

［Research Area］

1. Left-right asymmetric development in Drosophila
The internal organs of many animals show directional left-right(LR) asymmetry.
However, mechanisms of LR asymmetricdevelopment remain largely unknown in most animals. Drosophila,
a fruit fly, is a good model organism for studying developmental
biology. We aim to understand the mechanisms of LR asymmetricdevelopment, such as chirality of cells, using combinations ofgenetics, computer simulation, and bioimaging.
2. Mechanisms of Notch signaling
Development and homeostasis require cell-cell interactions in
multicellular organisms. Notch is a receptor and transduces cellsignal through a direct cell-cell interaction. We are studying cellsignaling through the Notch receptor using Drosophila as a model
system. We aim to understand the mechanisms of Notch signaltransduction and find ways to control the Notch signaling.
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Laboratory of Comparative Neurobiology
Members

Sakiko SHIGA (Prof), Masaharu HASEBE (Asst Prof), Yoshitaka HAMANAKA (Asst Prof), Aisa
SAKAGUCHI （Asst Prof）Xi Jili (Specially Apointed Asst Prof)

TEL・FAX

TEL:06-6850-5423

Home Page

https://www.bio.sci.osaka-u.ac.jp/bio_web/lab_page/shiga/［Research Interests］
Animals and plants are organized on a daily and seasonal schedule.
By using endogeneous clock system organisms anticipate andprepare for environmental harsh period to change their
physiological conditions. We study neuronal mechanisms
underlying biological timing system.
1) Photoperiodism and diapause
For seasonal adaptation animals and plants read day length tochange their morphs or development. This is called
photoperiodism. We study photoperiodic mechanisms using insects(flies, true bugs, a silkworm) and a mollusk. The blowfly
Protophormia terraenovae develop the ovaries under long days but
suppress their development to enter diapause under short days
(Figure). We have identified circadian clock neurons involved inphotoperiodic response and different types of brain neurosecretory
neurons controlling diapause in P. terraenovae. However, itremains unknow how the photoperiodic clock system discriminates
between short and long days (time measurement) and counts
number of days required for switching diapause and nondiapause
states (day counting). We investigate into time-measurement andday-counting system in the brain.

e-mailshiga.sakiko.sci@

2) Circa’bi’dian rhythm
The large black chafer Holotrichia parallela have a unique two-day
periodicity called circa’bi’dian rhythm. In the field they appear on
the ground to forage and mate every two nights. In the laboratory
the rhythm continues under constant darkness with a period about
48h. Phase responses of the rhythm to light pulses suggest thecircadian clock (ca 24 h) produces circa’bi’dian rhythm (ca 48 h).
We propose a novel function of the circadian clock characterized
by the release of an output signal every two cycles to produce the 2day rhythm. We are interested in proximate and ultimate causationof the circabidian rhythm.

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Cellular Life Science
Members

Naotada ISHIHARA (Professor), Emi OGASAWARA (Assistant Professor),
Yuichi MATSUSHIMA (Specially Appointed Assistant Professor)

TEL・FAX

Tel: 06-6850-6706

Home Page

https://mitochondria.jp/englishpage

e-mailnaotada@bio.sci.

［Research Area］
Mitochondria, double membrane-bound organelles
with tubular network structures, are essential foroxidative ATP production and play pivotal roles inregulating calcium homeostasis, ROS production andapoptosis. Mitochondria dynamically change theirmorphology by frequent fusion and fission, and three
types of high molecular-weight GTPase proteins havebeen identified as core components of the fusion andfission machineries. We are analyzing their molecularmechanism and the physiological roles in mammals,
and found that the regulation of mitochondrial
dynamics coupled with a quality control system isessential for cellular homeostasis, mtDNA regulation,and tissue differentiation. To analyze mitochondrial
dynamics, we characterize purified proteins, observe
live imaging, and analyze in vivo phenotypes inmitochondrial-dynamics defective cells/animals.
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Laboratory of RNA Biofunction
Members
TEL
Home Page

Tetsuro HIROSE (Professor), Tomohiro YAMAZAKI (Lecturer), Kensuke NINOMIYA (Lecturer)
hirose.tetsuro.fbs@
e-mail
TEL: 06-6879-4674
http://www.fbs.osaka-u.ac.jp/labs/hirose/［Research Interests］

Transcriptome analyses in the beginning of the 21st
century have revealed that large portions of the eukaryotic
genomes produce numerous non-coding RNAs (ncRNAs),
which expectedly play important regulatory roles in various
biological events. Our laboratory aims to elucidate thefunctions and the underlying new genetic code, therebyreconstructs the basic concept of genome function. Among
thousands of ncRNAs in mammalian cells, we particularly
focus on “architectural ncRNAs (arcRNAs)” that playarchitectural roles to build membraneless organelle throughinduction of intracellular phase separation. We attempt toelucidate the specific biological functions of the arcRNAs byoperating the massive phase-separated structures.

Graduate School of Science
2023-2024

Department of Biological Sciences

Laboratory of Animal Morphology
Members

Hidetaka FURUYA (Professor), Atsuko YAMADA (Assistant Professor)

e-mailhfuruya@bio.sci.

Home Page

http://www.bio.sci.osaka-u.ac.jp/dbs01/re-paper-temp.php?id=5［Research Area］
Organisms are quite small, but the most complicated creations in nature.
My lab is interested in reading the meaning of animal forms and uses
comparative anatomical approaches to understand the morphologicalevolution and adaptation. We are studying how the animal form had
evolved in the life history using the dicyemid mesozoans (Phylum
Dicyemida), a unique group of animals that inhabit the renal organ of
cephalopod mollusks. The dicyemid body consists of only 20 to 40 cells
and represents the smallest number of cells in the animal kingdom.
Dicyemids have neither body cavities nor differentiated organs, and werenamed "Mesozoa" for the dicyemids as an intermediate between Protozoa
and Metazoa in body organization. However, some zoologists regard thesimple organization of dicyemids to be the result of specialization ofparasitism. Recently we have revealed that dicyemids are not truly
primitive animals, that deserve the name of “mesozoans”, but that they
belong to the metazoans. It still remains to be explored how such a simple
body organization has evolved. Dicyemids are subjected to a number of
selecting pressures due to their unique habitat with the renal organs of
cephalopod hosts. In terms of morphological and ecological adaptation, thismicroenvironment could afford a space for a simple natural experiment.

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Laboratory of Photosynthetic Biology
Members

Hirozo Oh-oka (Professor)

TEL・FAX

06-6850-5424

Home Page

https://www.bio.sci.osaka-u.ac.jp/~ohoka/eng/index_e.html[ResearchArea]
All life activities on the earth are supported by the
sun's inexhaustible light energy. Photosynthesis is an
important biological reaction system that is
indispensable for maintaining the current global
environment, efficiently converting light energy into
chemical energy that can be used by living organisms.
Our research seeks to understand this light-energy
conversion mechanism at the molecular level and to
explain it using terms of physics and chemistry.
The photosynthetic reaction center complexes, which
are membrane proteins, are responsible for theprocess of light energy conversion by plants andphotosynthetic microorganisms. In the complexes,
absorbed light energy is transferred to the dimericchlorophyll pigments (special pair of P), which isthen excited to P* and forms a charge-separated stateof P+A- between the special pair and the primaryelectron acceptor (A). The energetic electrons arethen transferred through various electron-transfer

e-mailohoka@bio.sci.

components in a bucket relay-like fashion, eventually
producing the reducing power (NADPH) necessary
for the anabolic reaction. We are using biochemical,
spectroscopic, and molecular biological techniques to
elucidate the reaction mechanisms of light-energy
conversion.

Arrangement of photosynthetic pigments inheliobacterial reaction center. The P800 is
consisted of a dimeric (BChl g)2.

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Interdisciplinary Biology 1
Members

Takuro NAKAGAWA (Associate Professor), Yumiko KUBOTA (Associate Professor)

E-mailnakagawa.takuro.sci@, ykubota@bio.sci.,

Home Page

https://www.bio.sci.osaka-u.ac.jp/~takuro/science/markdown/
https://www.bio.sci.osaka-u.ac.jp/~ykubota/Top.html

Mechanism of Chromosome Rearrangement– Takuro NAKAGAWA –An extremely large number of repetitive sequences arepresent in a eukaryote genome. Intriguingly, repetitive
sequences occupy around half of the human genome. Gross
chromosomal rearrangement (GCR) such as translocationoccasionally occurs using the repetitive sequences as “DNAglue”. GCR can cause genetic diseases including cancer andcell death. From the evolutional point of view, on the other
hand, GCR can be one of the driving forces of evolution.
Therefore, GCR appears to be the integral phenomenon ofliving organisms. Using fission yeast as a model organism,
we are trying to identify the genes that suppress or promote
GCR and elucidate the molecular mechanism of GCR.
Fluorescent image of fission yeast:
The centromere region of chromosomesthat contain DNA repeats.

Initiation of DNA Replication in Eukaryotic Cells– Yumiko KUBOTA –One of most fundamental feature of life is reproduction. Allliving organisms are made up of a cell or cells and DNA in cell
nuclei carries the genetic information of the organisms toconstruct and maintain them. Therefore, the precise duplicationand distribution of DNA to daughter cells during cell division
cycle is the basis of keeping an organism alive. The failure ofthese processes would cause the severe defect in the organisms,
such as cell death or serious diseases like cancer. To understandthe faithful duplication of DNA, we investigate the basic
mechanisms and the regulations of initiation of DNA replication
using the cell-free DNA replication system of Xenopus egg
extracts, which contain plentiful proteins for DNA replication to
support the rapid early cell division cycle of embryo.
Replicated DNA visualized
by incorporation of labeled
nucleotides.

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Laboratory of Interdisciplinary Biology 2
Members

Kaoru IMAI (Associate Professor), Tetsuhiro ASADA (Assistant Professor)

e-mailimai@bio.sci., tasada@bio.sci.

Home Page

https://www.bio.sci.osaka-u.ac.jp/~tasada/Site05/

Molecular and Celllar Analysis of Ascidian Embryogenesis– Kaoru IMAI –Our body developed from a fertilized egg that is only 100
microns in size. How do cells with different functions develop
from a fertilized egg, which is only a single cell, to form awell-organized body? In our laboratory, we are using molecularbiology techniques to study the mechanism of how the bodydevelops from the egg, using the sea squirt as a modelorganism.

Mechanisms of cell’s division-plane selection and tissue
formation in plants – Tetsuhiro ASADA –Cell arrangement in plant bodies largely depends on theselection of the plane of cell division. As an effort tounderstand the mechanisms of controlling the plane of cell
division for plant tissue formation, we analyze the tendencies
of division plane selection in isolated cells and developing
tissues from plants.

Graduate School of Science
2023-2024

Department of Biological Sciences

Laboratory of Synaptic Plasticity
Memberｓ

TEL
Home Page

Keiko TOMINAGA（Associate Professor）
TEL:06-6879-4662

e-mailtomyk@fbs.

https://rd.iai.osaka-u.ac.jp/ja/d5bbff3350025e27.html［Research Theme］

Most living things on the earth have the circadian clock(biological clock) to adapt to the daily environmental
changes. In mammals, the master circadian clock is located in
the suprachiasmatic nucleus (SCN) in the hypothalamus. The
master clock synchronizes its autonomous oscillation with theenvironmental changes corresponding with the day-nightcycle, and adjusts the internal environment with the external
environment regulating the peripheral clocks in other brain
regions and the body (right figure). We aim to elucidate howvarious environmental factors including light affect thebiological clock at the molecular level. In addition, we are
studying the aftereffects of those factors, that is, plasticity ofthe biological clock.
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Laboratory of Organic Biochemistry
Members

Yasuhiro FUNAHASHI (Professor), Masaki NOJIRI (Associate Professor), Tsubasa HATANAKA (Assistant Professor)

TEL・FAX

06-6850-5767

Home Page

http://www.chem.sci.osaka-u.ac.jp/lab/funahashi/index.html［Research Interests］
1) Synthesis of dinuclear and multinuclear metal
complexes activating molecules2) Synthesis of heterometallic multinuclear complexes
activating molecules
3) Synthesis of novel metal complexes as aphotosensitizer4) Development of artificial metalloenzymes activating
molecules
5) Investigation of relationships between structures andfunctions of metalloprotein
6) Synthetic and mechanistic study on metal complexes
with anticancer activity

e-mailfunahashi@chem.sci.

molecules such as O2 and N2. The 1st transition metals are
frequently essential trace elements for organisms, working at
the active sites in the proteins. The metal complexes sometimes
show pharmaceutical activity. We study on metals in biology,
and we newly develop relevant metal complexes andmetalloenzymes.

The photosynthetic energy transduction and metabolism
involve photo-excitation coupled with electrontransfer process, and activation of substrates including
small mo

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Macromolecular StructureMembers
Home Page

Katsumi IMADA (Professor), Fumitoshi KANEKO (Associate Professor),
Tatsuya KAWAGUCHI (Lecturer), Norihiro TAKEKAWA (Assistant Professor)
http://www.chem.sci.osaka-u.ac.jp/lab/imada/en/index.html［Research Area］

Biological process is driven by complex molecular machines
composed of biological macromolecules. The flagellum, which is anorganelle for bacterial motility, is one of those molecular machines.
The flagellum is a huge protein assembly composed of a helicalfilamentous screw, a molecular universal joint, a highly efficient iondriven motor and a protein export apparatus for self-construction.
The Laboratory of Macromolecular Structure aims to provide
fundamental understanding of operating principles and the selfassembly mechanism of biological macromolecular machines, suchas the bacterial flagellum, through the studies of molecular structure
at atomic resolution and reconstitution of the molecular machines.
We also study structures of polymer complexes with low molecularweight compounds and the relationship between their structures andfunctions.
1) Rotation mechanism of bacterial motor systems.
2) Self-constitution mechanism of bacterial motility machines.
3) Structural and functional studies on bacterial infection
apparatus.

e-mailkimada@chem.sci.

4) Structural and functional studies on environmental
sensing units.
5) Study on the structure of polymer complex withsmall molecule and its formation mechanism.

Schematic drawing of the bacterial hook basal-bodyarchitecture

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Laboratory of Supramolecular Functional
ChemistryMembers

Hiroyasu YAMAGUCHI (Professor) , Yuichiro KOBAYASHI (Assistant Professor)

TEL・FAX

Tel: 06-6850-5460 ・ Fax: 06-6850-5457

Home Page

http://www.chem.sci.osaka-u.ac.jp/lab/yamaguchi/english/index.html

e-mailhiroyasu@chem.sci.

［Research Interests］
1) Development of a high performance sensing element.
2) Construction of energy conversion and catalytic systems
using hybrids of biomacromolecules with synthetic
molecules.
3) Creation of functionalized supramolecular materials
based on self-assembly of bio-related and/or synthetic
polymers.
In biological systems, life processes are led by the uniquebehavior of macromolecules such as proteins and DNA.
Molecular recognition by macromolecules plays an importantrole, for example, in substrate specificity of enzymes andantigen-antibody reactions in human life. Selective molecular
recognition among macromolecules is achieved through a large
number of weak interactions. We have focused our attention on
the special behavior of antibodies, especially monoclonal
antibodies, because they can recognize a larger and more
complex compound with high specificity. In this laboratory, wedevelop novel supramolecular materials and construct
functionalized sensing, catalytic, and energy conversion systems
via specific molecular recognition of biomacromolecules andselective assembly of bio/synthetic molecules.

Graduate School of Science
2023-2024

Department of Biological Sciences

Laboratory of Macromolecular Solutions
Members

Ken TERAO (Professor)

Home Page

https://www.chem.sci.osaka-u.ac.jp/lab/terao/[Research Area]
Macromolecules in solution can take a nearly infinite number ofconformations due to their high degree of freedom of internal rotations.
Macromolecules in solution have, therefore, specific characteristics notfound in small molecules. Intramolecular interactions in a macromoleculeand intermolecular interactions with solvent molecules significantly
influence the molecular shape in solution. Furthermore, strong
intramolecular interactions, including hydrogen bonding and electrostaticinteractions, lead to the formation of micelles and aggregates. Theintermolecular interactions between polymers through solvents can also
cause various phase separations. Such phenomena correlate with thefunctions in biosystems. Our research aim is to clarify the various
phenomena exhibited by macromolecules in solution, that is, single chain
conformation, complex formation behavior, and phase separation
behavior by using the latest scattering and spectroscopic methods.
[Research Projects]
1) Conformation and molecular recognition ability of polysaccharides
and their derivatives
2) Molecular conformation and intermolecular interactions of ring andbranched polymers
3) Aggregation and phase separation of branched polymers-poor solvent
systems4) Complex formation of polymers with nanoparticles

Biomolecular Machine Design Group
Members

Ken’ya FURUTA (Guest Associate Professor)

TEL・FAX

078-969-2214

Home Page

http://www.nict.go.jp/frontier/seitai/index.html

e-mailFurutak nict.go.jp

Top: Sorting with nanomachines(Ibusuki et al., Science 2022)。

[ResearchArea]- Design principles of biomolecular motors
In an environment governed by thermal fluctuations,
it seems difficult for a protein to move unidirectionally. In addition to analyzing existing
biomolecular motors, we are trying to establish aconstructive approach by combining simple domains
into a new biomolecular motor prototype andobserving how it behaves.
- Design and control of collective dynamics
Individual molecular motors cannot explain many
biological phenomena. To address this, we are
creating experimentally accessible model systems
using DNA nanostructures and other biologicalmaterials to explore the collective dynamics.
- Design of autonomous micro-robots
The 3 key elements of a robot are sensors, processors,
and actuators. Cells are equipped with these elements

Bottom: Autonomous micro-robots(Furuta et al., Curr Opin Biotechnol2017)。

and can be viewed as micro-robots that moveautonomously. We aim to understand themechanisms by which cells remember informationand make decisions based on that memory, through asynthetic biology approach―the creation of suchmicro-robots by assembling structures using
biological materials and self-assembling techniques.

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory for Molecular and Developmental
Biology(Institute for Protein Research)
Members

Takahisa FURUKAWA (Professor), Taro CHAYA (Associate Professor),
Hung-Ya TU(Assistant Professor)

TEL・FAX

Tel: 06-6879-8631・Fax: 06-6879-8633

Home Page

http://www.protein.Osaka-u.ac.jp/furukawa._lab/en/index.html[Research Interests]
Our laboratory studies molecular mechanisms underlying thedevelopment and function of the vertebrate central nervous
system(CNS) using various research methods of molecularbiology, mouse genetics, biochemistry, cell biology and neuralphysiology. We use the retina as a model system to understandhow DNA encodes programs to generate various neurons andglial cells, form precise neuronal circuits, and enable
complicated neuronal function. We also focus on how
abnormality of biological processes in development andmaturation leads to human diseases. We are eager to contributeto development of diagnosis and cure of human diseases.
Together, our lab aims to elucidate mechanisms and principles
underlying the CNS development from DNA programs tophysiological function and human diseases.

e-mailtakahisa.furukawa@protein.

2) Elucidation of functional roles of microRNAs (miRNAs)in CNS development.
3) Analysis of molecular mechanisms underlying transcription
and chromatin regulation in neuronal differentiation.

[Research Project]
1) Molecular analysis of synapse formation in the CNS.

Figure. We previously identified Pikachurin, an extracellularmatrix–like retinal protein, and observed that it localized to thesynaptic cleft in the photoreceptor ribbon synapse. Pikachurin
KO mice showed improper apposition of the bipolar cell
dendritic tips to the photoreceptor ribbon synapses, resulting inalterations in synaptic signal transmission and visual function.
WT (left), Pikachurin KO (right)
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Laboratory for Biomolecular analysis(Institute for Protein Research)

Members

Nobuaki Okumura

TEL・FAX

06-6879-4312

Home Page

http://www.protein.osaka-u.ac.jp/metabolism/taisha.html

e-mailnokumura@protein.

［Research Programs］(1) Metabolism and function of dipeptides in mammals(2) Proteomic analysis of protein and peptide breakdown
In living cells, there are numerous short peptides such as dipeptides andtripeptides, some of which are produced by protein degradation, while theothers synthesized from amino acids by specific enzymatic reactions.
Regardless of their route of production, short peptides are essential toprotein metabolism and its homeostasis. We have been studying thefunction and metabolism of short peptides, especially focusing on
dipeptide-hydrolyzing enzymes or dipeptidases, CN1 and CN2.
We have also been trying to develop proteomic procedures to analyze
protein degradation, and apply them to study disease-induced changes inprotein degradation products

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Organelle Biology(Institute for Protein Research)

Members

Masato NAKAI (Associate Professor)

TEL・FAX

TEL:06-6879-8612 FAX:06-6879-8613

Home Page

http://www.protein.osaka-u.ac.jp/enzymology/

e-mailnakai@protein.

［Research Interests］
In plants and algae, the eukaryotes, photosynthesis is carried out
in a specialized organelle called chloroplast. It is now widely
accepted that virtually all chloroplasts in today’s photosynthetic
eukaryotes derive from one fairly rare primary endosymbiotic
event with a cyanobacterium-like ancestor thought to haveoccurred more than a billion years ago. Extant higher plants can
synthesize only ~100 proteins inside the chloroplast but must
import such 2000-3000 different cytosolically-synthesized
nuclear-encoded proteins, across the double envelope
membranes surrounding this organelle, to fulfill their complex
physiological roles including photosynthetic functions. Two
successive protein translocons at the outer and inner envelope
membranes, termed TOC and TIC, respectively, are responsible
for the task of protein import into chloroplasts. Our recent
discoveries of the genuine TIC translocon (SCIENCE 2013) andassociated import motor (PLANT CELL 2018) both of which are
well conserved among most land plants as well as green algae
could provide us an entirely revised view on the molecularmechanisms of protein translocation across the inner envelope
membrane of chloroplasts and also novel insights on theevolution of the chloroplast protein import system.

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Laboratory of Protein Synthesis and Expression(Institute for Protein Research)
Members

Junichi TAKAGI(Professor), Takao ARIMORI (Associate Professor)

TEL・FAX

TEL:06-6879-8607・FAX:06-6879-8609

Home Page

http://www.protein.osaka-u.ac.jp/rcsfp/synthesis/index.html

e-mailtakagi@protein.

[Research Interests]
1) Elucidation of mammalian signal transduction mechanism via structural study of ligand-receptor complexes2) Structure-based design of “novel therapeutic proteins” through state-of-the-art protein/antibody engineering
3) Near-atomic resolution structural analysis of biologically important macromolecules by using cryoelectron microscopy (cryo-EM)
Cellular response to the extracellular environment depends on the “sensing” the extracellular cues by use of the receptor-ligand system.
Binding of ligands to the extracellular domain of the receptors transduce signals into cells that initiates various cellular events, ultimatelychanging the cell fate. Most of the “signal transduction researches” deal with cytoplasmic events such as phosphorylation/dephosphorylationof signaling molecules and subsequent recruitment of adapter molecules, but mechanism for the “signal transmission across the membrane”,
the very first step in the signaling pathway is poorly understood.
Our study focuses on questions such as how receptors recognize their
specific ligands, how this recognition leads to structural change in thereceptor complex, and how the information cross the plasma membranewithout transporting chemical entity. Using structural as well as
chemical approach, we would tackle on this difficult problem to obtaininsights into the mechanism of transmembrane signaling. Suchinformation would eventually be used for drug development and benefit
medical as well as biological research in general.

Crystal structure of human Wnt3 (left) and cryo-EM structure of LRP6
(center), combined to give hypothetical structure of the entire signaling
machinery on cell surface (right).

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory for Computational Biology(Institute for Protein Research)
Members

Kenji MIZUGUCHI (Professor), Kosuke HASHIMOTO (Associate Professor),
Chioko NAGAO (Assistant Professor), Reiko WATANABE (Assistant Professor)

TEL・FAX

Tel: 06-6105-6961, Fax: 06-6105-6962

Home Page

https://mizuguchilab.org/

e-mailkenji@protein.

[Research Area]
1) Data integration for relating molecular-level events to higherorder biological systems.
2) Understanding and predicting molecular interactions involving
proteins, modelling biological responses.
3) Transcriptome analysis of early human embryos.
4) In silico prediction of pharmacokinetic parameters.

Virtual screening
Pharmacophore modeling

BioassayInteraction analysis

Viability（%）

Activity（%）

We aim to increase our understanding of biological systems anddiseases by combining computer science and computational
chemistry approaches, with applications to drug discovery andother research areas. Artificial Intelligence (AI) is expected toplay major roles in many domains. Recognizing that theavailability of a large amount of data in a computer-friendly
format is key to the successful development of AI models, ourresearch is focused on integrating a wide array of data,
including genes, proteins, chemical compounds and diseases.
We also develop methods for predicting protein structure,function and interaction, and apply them to to specific biologicalproblems.

Compounds

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Laboratory of Supramolecular Crystallography(Institute for Protein Research)
Members

Atsushi NAKAGAWA (Professor) , Eiki YAMASHITA (Associate Professor), Mamoru SUZUKI(Associate Professor), Makoto MATSUDA (Specially Appointed Assistant Professor)

Home Page

http://www.protein.osaka-u.ac.jp/rcsfp/supracryst/en[Current Research Projects]
1) X-ray structure determination of biological macromolecularassemblies and proteins.
2) Development methodologies for X-ray structure determinationof biological macromolecular assemblies using synchrotron
radiation.
3) Development of data processing algorithm of diffraction datafrom large unit cell crystals and micro-crystals.

Major research targets include drug efflux complexes thatplay an important role in drug resistance in Pseudomonas
aeruginosa, one of the bacteria causing hospital-acquired
infections, Rice dwarf virus with a molecular weight of 75
million, PfV, a virus-like particle that forms stable sphericalparticles even under high temperature conditions of over 90
˚C.

Our laboratory aims to elucidate the molecular interactions andmolecular recognition mechanisms that are important forunderstanding biological functions based on precise atomic
structures. For this purpose, X-ray crystallography and cryoelectron micrography are used.

SPring-8 BL44XU

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Protein Profiling and Functional
Proteomics(Institute for Protein Research)
Members
Home Page

Toshifumi TAKAO (Professor), Koki SAKURAI (Assistant Professor)
http://www.protein.Osaka-u.ac.jp/rcsfp/profiling[Research Programs]1) Development of chemical/analytical methods and software foranalysis of protein primary structure by mass spectrometry2) Mass spectrometric analysis of post-translational modifications3) Development of chemical and analytical methods for proteomics
4) Study on fragmentation of peptides and carbohydrates in mass
spectrometry5) Hardware development for high-sensitivity and high-accuracy
mass spectrometry

biological events. We apply the following developed
methods to the structural analysis of micro quantities of
peptides, proteins, and their related substances.

Mass spectrometry (MS) is a well-accepted technique for the
analysis of chemical structures of biological compounds. For the last
four decades, we have been working to develop methods fordetermining primary structures and post-translational modificationsof proteins using MS. In conjunction with accumulating protein andgene sequence databases, we are using state-of-the-art MS for largescale protein identification, which is indispensable for understanding
MALDI-TOFMS can reveal the peptide Cterminus.

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Laboratory of Genome and Chromosome
Functions(Institute for Protein Research)
Members

Akira SHINOHARA (Professor), Asako FURUKOHRI (Associate Professor),
Masaru ITO (Assistant professor)

TEL・FAX

Tel: 06-6879-8624 ・ Fax: 06-6879-8626

Home Page

http://www.protein.osaka-u.ac.jp/genome/english/

e-mailashino@protein.

［Research Area］[Research Subjects]
1) In vivo and in vitro analysis of recombination reactions
2) Analysis of proteins working with RecA homologues inrecombination
3) Analysis of the roles of chromatin modification in meiotic
recombination
4) Mechanisms of choice of DSB repair pathways
5) Analysis of recombination in human cells6) Mechanism of chromosome dynamics in mouse meiosis
Homologous recombination, an exchange between DNA strands, plays arole in the maintenance of genome stability and the production of
genome diversity. While, in mitosis, it is required for the repair of DNA
damage, it is for the segregation of homologous chromosome at meiotic
division I. Meiotic recombination is coupled with chromosome of therecombination leads cancer and infertility in human. To reveal molecularmechanism of the recombination,

we have been analyzing genes/proteins involved in the processusing molecular, genetical,biochemical, and structural methods.

Synaptonemal complex (SC) formation. Immuno-staining analysis of the SC
components, SYCP1 (red) and Mlh1 (green) in the mouse spermatocyte. In
SCs, paternal and maternal chromosomes are fully paired along chromosomes.
Blue shows DNA, thus chromosomes. X-Y pair is shown in blue.

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory of Protein Crystallography(Institute for Protein Research)

Members

Genji KURISU (Professor), Hideaki TANAKA (Associate Professor),
Akihiro Kawamoto (Assistant Professor), Naoko NORIOKA (Technical Assistant)

Home Page

http://www.protein.osaka-u.ac.jp/crystallography/EngHP/[Research Interests]
1)
2)
3)

Structural studies of photosynthetic energy-transducing membraneprotein complex and related redox enzymes
Crystal structure analyses of dynein motor
Damage-free crystal structure analysis of metalloproteins at highresolution

Three-dimensional protein structure brings us a deeper insight into the
biological function. X-ray crystallography combined with Cryo-TEM isthe best method to determine atomic coordinates of protein molecules.
The main aim of our group is the structure determination of the biologicalmacromolecular assemblies including membrane protein complexes, inorder to elucidate the molecular mechanism of the highly organizes
biological process at atomic level.

Crystal Structure of the dynein motor domain

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Laboratory of Protein Organic Chemistry（Institute for Protein Research）
Members

Hironobu HOJO (Professor), Toshiki TAKEI (Assistant Professor), Shun ITO (Assistant Professor)

TEL・FAX

Tel: 06-6879-8601・Fax: 06-6879-8603

Home Pagee-mailhojo@protein.

https://sites.google.com/site/takatoshihikidalaboratory/home［Research interests］
1) Establishment of a method for protein
synthesis
2) Chemical synthesis of glycoprotein,
modified histone, and membrane protein
Chemical methods enable the synthesis of proteins,which can not be prepared by the recombinant method,such as site-specifically labeled, glycosylated andphosphorylated proteins. Our laboratory is aiming topromote new protein researches using these synthetic
proteins. Thus, our laboratory is developing facile
methods for protein synthesis based on ligation
chemistries. In addition, the synthetic method isapplied for the preparation of membrane proteins andtheir partial sequence

to elucidate the signal transduction mechanism bysolid state NMR and IR. Modified histones andtheir partial sequences, glycosylated proteins arealso synthesized for the functional analyses.

General procedure for the chemical protein synthesis.

Graduate School of Science
2023-2024

Department of Biological
Sciences

Laboratory for Advanced Brain Functions
Members
TEL・FAX
Home Page(Institute for Protein Research)

Takatoshi HIKIDA (Professor), Tom MACPHERSON (Assistant Professor),
Takaaki OZAWA (Assistant Professor)
e-mail hikida@protein.
TEL 06-6879-8621 /FAX 06-6879-8623
https://sites.google.com/site/takatoshihikidalaboratory/home[Research Interests]
Our laboratory studies neural circuit mechanisms
underlying various advanced brain functions such as
cognitive learning and decision making behaviors
using molecular techniques for neural circuit specificmanipulation. We use several mouse models to reveal
molecular pathologies of neuropsychiatric diseases.
Especially, we focus on molecular mechanisms ofgene-environment interaction in the pathogenesis of
mental disorders. We also promote translational
research for targeting mental disorders in collaboration
with clinical departments and pharmaceuticalcompanies.

[Research Programs]
1. Analysis of neural circuit mechanisms in advanced
brain functions
2. Molecular analysis of neuropsychiatric pathologies
3. Translational research of mental disorders

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Laboratory of CryoEM Structural Biology(Institute for protein research)

Members

Takayuki KATO(Professor), Jun-ichi KISHIKAWA(Assistant Professor), Hiroko
TAKAZAKI(Assistant Professor)

TEL・FAX

06-6105-6079

Home Page

http://www.protein.Osaka-u.ac.jp/cryoem/index.html

e-mailtkato@protein.

［Research Interests］(1) Study of energy conversion mechanism of molecular motor(2) Structural analysis of olfactory receptors(3) Study of molecular dynamics by cryo-electron microscope(4) Development of high-resolution structural analysis methodby cryo-electron microscope

Structure of Flagella Hook

The biomolecules such as protein and nucleotide are responsible
for life activity, its function is relative to the structure. In ourlaboratory, we will clarify the molecular mechanism by structural
analysis using a cryo-EM. In particular, we are analyzing theenergy conversion mechanism of motor protein such as flagellar
motors and ATPase, and the mechanism of olfactory receptors. We
are also developing of the method for analysis of molecular
dynamics by cryo-EM and for high-resolution and high-resolution
structural analysis by cryo-EM.

Graduate School of Science
2023-2024

Cryo-EMs

Department of Biological
Sciences

Laboratory for Cell Systems(Institute for Protein Research)

Members

Mariko OKADA (Professor), Keita IIDA (Associate Professor), Ayaka ICHIKAWA(Assistant Professor),

TEL・FAX

TEL: 06-6879-8617・FAX:06-6879-8619

Home Page

http://www.protein.osaka-u.ac.jp/cell_systems/index.html

e-mailmokada@protein.

[Research Theme] Understanding the dynamics ofcells as time and space network of molecules
Cells carry out various molecular controls and determine theirfate corresponding to the living environment. Upon theprocedure, characteristics of cells occur not only by the property
of molecule itself but also by the property of intercellular
dynamics. In our laboratory, we quantitatively analyze
interaction network of intracellular molecules such as protein,
RNA and DNA to reveal the mechanism of intracellular process
and cell fate control. We particularly focus on regulating gene
expression dynamics by intracellular signal transduction andtranscription factor. We thoroughly analyze the molecularmechanisms by combining the quantitative experimental analysis
of molecular activity against the input of the cell, mathematicalmodeling and simulation analysis. We also study data-driven cellsystems to understand how the original stimulus influences thewhole cell and activates self-control using comprehensive
measurement techniques such as genome, transcriptome,
epigenome and proteome.

Studying time development process of cells in proliferation anddifferentiation, we want to understand the logic structure toinduce cellular specificity by focusing on solving the signaltransduction and transcription responses. Our laboratory
conducts wet experiments along with dry approaches such as
computational science, mathematics, bioinformatics and deeplearning.
An integrative approachof wet lab experiments
and dry lab computation
reveals quantitative
mechanisms in cellular
information transmission
for cell fate control.

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Laboratory of Nanobiology(Institute for Protein Research)

Members
TEL
Home Page

Yoshie HARADA (Professor)
06-6879-8627

e-mailyharada@protein.

URL: http://www.protein.osaka-u.ac.jp/nanobiology/en/[Research Interests]
Development of methods for measuring intracellular heatproduction (temperature)
Temperature that changes with heat is one of the basic parameters
expressing the state of matter. However, it is not clear how heat andthe resulting temperature change can alter cellular function. To
measure the heat production and temperature changes within a single
cell, we developed various temperature probes that are based on
temperature-sensitive fluorescent polymers, fluorescent dyes,
fluorescent nanoparticles, and fluorescent nanodiamonds. We
combine various fluorescence imaging techniques such as
fluorescence lifetime microscopy and ratiometry. These newmeasurement methods aim to elucidate the significance anduniversality of released heat and local temperature changes in cells.
We are also conducting joint research on applications of our methods
to the biomedical field, such as the evaluation of heat treatment at thecellular level.

Intracellular temperature imaging using temperaturesensitive fluorescent polymers and the fuorescence
lifetime imaging microscopy.
The distribution of the color suggests the temperature
distribution within a cell.

Graduate School of Science
2023-2024

Department ofof Biological
Biological Sciences
Sciences

Laboratory for Ultra-High Magnetic Field NMR,
Molecular Biophysics (Institute for Protein Research)
Members

Yohei MIYANOIRI (Associate Professor)
Yoh MATSUKI (Associate Professor),

Tel・Fax

Tel: +81-6-6879-8598

Home Page

http://www.protein.osaka-u.ac.jp/biophys/index.html

y-miyanoiri@protein. ; yoh@protein.

e-mail［Research Interests］

Signal transduction and energy conversion play very
important roles in the human body. Many these functions
are performed by supramolecular systems acrossbiomembranes. These systems are also responsible forforming networks of integrated biological activities. We
are elucidating these essential functions of proteins on thebasis of structures, dynamics and the interactions revealed
mainly by nuclear magnetic resonance spectroscopy(NMR).

We are also developing NMR methods by using
advanced technologies for NMR experiments,
chemical biology, bioinformatics , molecular biology
and cell biology. Two NMR spectrometers featureshigh-power terahertz wave sources, gyrotron forenhancing the sensitivity by using electron spinpolarization, i.e., DNP.

NMR reveals structure and function of biologicallyimportant molecular complexes that not amenable to X-ray
crystallography and electron microscopy. These systems
include proteins bound to lipid bilayers and noncrystalline
large molecular complexes, such as membrane protein pHtrII
for the transmission of light signal, halorhodopsin for lightdriven ion pumping, amyloid protein fibers, and model Gprotein-coupled receptor (GPCR) complexes.

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Laboratory for Physical Biology(Institute for Protein Research)

Members

Madoka SUZUKI (Associate Professor)

TEL・FAX

06-6879-8628

Home Page

https://rd.iai.osaka-u.ac.jp/ja/ca5ca6ff0ffeeff2.html

Cells respond to heat in various ways through proteins
and their networks. What is the mechanism behindthese responses? Does the same mechanism apply tothe heat released by the cell itself?
We employ fluorescence microscopes and fluorescentprobes, develop multidisciplinary methods based on
quantitative imaging and opto-thermal technologies,
and apply the methods to biological systems ranging
from molecule to organism. Our aim is tocomprehensively understand heat, which is essential
for maintaining life of an organism and interacts withthe organism at all spatial scales. We are working on
both curiosity-driven projects in life science and thoserelated to diseases such as unstoppable thermogenesis
with local and international collaborators.

Spatial scale of a method［Research Interests］
Understanding the heat in biological systems
through quantitative imaging and perturbation ofprotein molecules, cells, and organisms

e-mailsuzu_mado@protein.

Commerciallyavailable
IR camera
Thermocouple
Higher spatial
resolution
Smaller subjects

mm
µm
nm
molecule
10 nm

cell
10 µm

PDB: 5GKZ

Graduate School of Science
2023-2024

tissue10 mmorganism
10 cm

Department of Biological
Sciences

Laboratory of Biomolecular Science andReaction(The institute of Scientific and Industrial Research)

Members

Shun’ichi KURODA (Professor), Toshihide OKAJIMA (Associate Professor), Yoh WADA (Associate
Professor), Kenji TATEMATSU (Assistant Professor), Masaharu SOMIYA (Assistant Professor)

TEL・FAX

06-6879-8460

Home Page

https://www.sanken.osaka-u.ac.jp/labs/smb/e-mailskuroda@sanken.

［Research Interests］
The aims of this laboratory are the analysis ofintermolecular reactions found in various biologicalphenomena, and the development of bio-industrially
useful technologies by utilizing these reactions.
1. In vivo pinpoint DDS nanocarriers using virus infection
machinery.
2. Single cell analysis by using automated single cell
analysis and isolation system.
3. Olfactory receptor repertory analysis by using human
OR cell array.
4. Elucidation of biogenesis of novel built-in type
cofactors.
5. Structural and functional analysis of bacterial twocomponent system.

Malignant tumor-specific DDS nanocarrier utilizing
sugar-lectin interactions.
(Left, high malignancy; Right, low malignancy)
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Laboratory of Homeostatic Regulation(Research Institute for Microbial Diseases)

Members

Tohru ISHITANI (Professor), Yuki AKIEDA (Assistant Professor),
Masayuki OGINUMA (Assistant Professor),

TEL・FAX

TEL:06-6879-8358・FAX:06-6879-8358

Home Page

https://ishitani-lab.biken.osaka-u.ac.jp

e-mailishitani@biken.

［Research Interests］
1.

A new concept of tissue homeostasis “Morphostasis”

2.

Aging programs and their regulation

3.

Robustness supporting signal transduction systems

4.

Molecular basis underlying “Diapause”, the systems
suspending vital activities

In our body, cells recognize their position and role and behave
accordingly via cell-cell communication. Such behavior
supports tissue morphogenesis and homeostasis, while its
dysregulation is involved in congenital malformation, cancer,
and aging. We focus especially on the cell-cell communication
and behavior supporting tissue homeostasis and explore
unknown molecular systems controlling embryonicdevelopment, organogenesis, regeneration, aging, anddisease, using in vivo imaging, animal model genetics,
molecular and cell biology, and biochemistry techniques.

Graduate School of Science
2023-2024

Department of Biological Sciences

Laboratory of Biohistory(JT Biohistory Research Hall [BRH])

Members

Zhi-Hui SU (Guest Professor), Chikara HASHIMOTO (Guest Professor), Hiroki ODA (Guest Associate Professor)

TEL・FAX

072-628-9750

e-mailsu.zhihui brh.co.jp (SU), hashimoto brh.co.jp (HASHIMOTO), hoda brh.co.jp (ODA)

Home Page

http://www.brh.co.jp[Research Area]
1) Insect-plant interactions and evolution2) Degenerative evolution of insect flight function
3) Origin and evolution of cell and developmental systems
in multicellular animals
4) Mechanism of chordata gastrulation
5) Relationship between cell cycle and differentiationbasis of our researches and also disseminate it. In the
Biohistory Group, we are conducting research on theabove five topics in evolutionary and developmental
biology.

By deciphering the historicity, diversity, andcommonality of living things written in genomes, we
conduct experimental researches on development,
evolution, and ecosystems of living things, as well as
research on expression of study results. By investigating
diverse organisms without focusing on individual genes
or species, we believe that the fundamentals ofdevelopment and speciation in the process of evolution
can be revealed. We place the love of living things at theLaboratory of Biomolecular Informatics(RIKEN Center for Biosystems Dynamics Research)

Members

Li-Kun PHNG (Guest Associate Professor), Kyogo Kawaguchi (Guest Associate Professor)

TEL・FAX078-306-3195 (Phng), 078-306-3354 (Kawaguchi)Home Page

https://www.bdr.riken.jp/

e-maillikun.phng

riken.jp, kyogo.kawaguchi

riken.jp［Research Interests］
1) Mechanisms of blood vessel formation (Phng).

We investigate molecular and mechanical mechanisms of
how endothelial cells shape blood vessels. We employ thezebrafish embryo as a model system, and perform highresolution fluorescent live imaging, genetic engineering,chemical and optical perturbations with numericalsimulations to understand how endothelial cells behave
during vessel morphogenesis (Fig. 1) and respond tohaemodynamics during development and homeostasis.

Fig 1: Actin cytoskeleton in a zebrafish vascular network.

2) Elucidating of hidden rules in multicellular phenomena

and cell differentiation(Kawaguchi)
We are broadly interested in biological phenomena that arise asa result of collective dynamics. We combine theoreticalphysics, cell culture experiments, and various data analysis
methods to elucidate the mechanisms by which tissues undergo
rapid turnover during in homeostasis, how cells collectively
flow in during development, and the laws that govern the
biological condensates that are born and disappear inside cells.

Fig 2: Skin stem cells undergoing rapid turnover in adult tissue

Graduate School of Science
2023-2024