EMBO/soda-nel huggingface dataset:
Receptor guanylyl cyclase‐G is a novel thermosensory protein activated by cool temperatures (2014)
Figure 6

Attenuation of coolness‐induced responses in the GG of GC‐G‐deficient (GC‐G‐KO) mice

A–H In situ hybridization experiments with an antisense probe for c‐Fos on coronal sections through the GG of wild‐type (WT; left panel) or GC‐G‐KO (right panel) mouse pups (P0–P4) exposed to warm (35°C; A–D) or cool (22°C; E–H) ambient temperature for 2 h. Panels (C, D, G, H) show higher magnifications of the boxed areas in (A, B, E, F). At 35°C (A–D), no c‐Fos expression was detectable in the GG of both WT (A, C) and GC‐G‐KO (B, D) individuals. Upon exposure to 22°C, strong c‐Fos expression was observed in the GG of WT pups (E, G), whereas c‐Fos expression was barely detectable in the GG of GC‐G‐KO animals (F, H). The data shown are representative of 10 independent experiments. Pups originated from six different litters for each genotype. Scale bars: 200 μm in (A, B, E, F); 50 μm in (C, D, G, H).
I Quantification of c‐Fos‐positive GG cells in WT and GC‐G‐KO pups on exposure to 22°C for 2 h. All stained cells on every section along the rostrocaudal extent of the GG were counted; the results shown are based on the above‐mentioned 10 experiments. The number of c‐Fos‐positive cells in the GG of a GC‐G‐KO mouse was determined relative to that in a concomitantly processed WT pup; the latter number was set to 100%. Data are mean ± SD (n = 11 in each genotype), **P 0.0001.
J–N Calcium imaging of coronal sections through the GG of olfactory marker protein‐green fluorescent protein (OMP‐GFP)/GC‐G+/+ or OMP‐GFP/GC‐G‐KO pups (P1–P4). High magnification image (J) of a tissue slice through the GG of an OMP‐GFP pup with GG neurons labeled by intrinsic GFP fluorescence (GFP fluorescence was merged with the transmitted‐light channel). Cells analyzed are circled in blue (GFP‐negative) or red (GFP‐positive). NC, nasal cavity. Scale bar: 30 μm. (K–M) Representative ratiometric Ca2+ transients induced by cooling from 37 to 15°C in GFP‐negative non‐neuronal cells (K) and in GFP‐positive GG neurons from OMP‐GFP/GC‐G+/+ (L) and OMP‐GFP/GC‐G‐KO pups (M). The numbers in the bottom right hand corners are the number of cells with Ca2+ transient similar to what is shown in the respective graph (left) and total number of measured cells (right). (N) Quantification of coolness‐induced ΔF in GG neurons from OMP‐GFP/GC‐G+/+ and OMP‐GFP/GC‐G‐KO mice. Coolness‐induced ΔF was calculated by subtracting the baseline fluorescence ratio (340/380 nm) at 37°C from the peak fluorescence ratio (340/380 nm) measured at 15°C. For OMP‐GFP/GC‐G+/+, the 29 coolness‐responsive neurons (black bar) of all 54 analyzed neurons (gray bar) from five slices (obtained from different animals) were analyzed. For OMP‐GFP/GC‐G‐KO, the 50 analyzed neurons (shaded bar) from five slices (obtained from different animals) were analyzed. Data are mean ± SD, **P 0.01.
Receptor guanylyl cyclase‐G is a novel thermosensory protein activated by cool temperatures (2014)
Figure 7

Impaired coolness‐evoked ultrasonic vocalization (USV) in GC‐G‐KO mice

A Reduced responsive rate of coolness‐stimulated USV in GC‐G‐KO pups. Pups were removed from their littermates and dams at postnatal (P) day 2, 4, and 6 and exposed to 15°C. USV was measured by use of the Anabat SD1 Bat detector. The number of responsive pups versus total number of pups tested for each WT and GC‐G‐KO group at different ages is indicated on the top of each bar. *P 0.05.
B, C Total number of USV calls (B) and response latency (C) in GC‐G‐KO and WT pups at P2. The horizontal bars indicate the mean. *P 0.05; **P 0.01.
Systemic autophagy insufficiency compromises adaptation to metabolic stress and facilitates progression from obesity to diabetes (2014)
f1

(a) Atg7+/− mice were generated as described in the Methods. PCR was done employing genomic DNA and primers flanking the floxed Atg7 regions. Arrows indicate wild-type Atg7 band in Atg7+/+ mice, increased size of PCR band due to inserted flox sequence in Atg7F/+ mice and decreased size of PCR band due to Cre-mediated deletion in Atg7+/− mice, respectively. (b) RT–PCR (left) and real-time RT–PCR (right) were performed using total RNA prepared from tissues of Atg7+/− or control Atg7+/+mice, and primers specific for Atg7 or β-actin sequence. Fold changes of the RT–PCR band intensities are shown (left). *P0.05, **P0.01, ***P0.001; Student’s t-test, n=3. (c) Tissue lysate from fasted 12-week-old Atg7+/− and control Atg7+/+mice was subjected to immunoblot analysis using anti-LC3 or -p62 antibody. Fold changes of the immunoblot band intensities are shown (middle and right). **P0.01, ***P0.001; Student’s t-test, n=3. (d) Cell lysate of Atg7+/+, Atg7+/− and Atg7−/− MEFs was subjected to immunoblot analysis using antibodies specific for LC3 and p62 after rapamycin (Rap) or control solvent (dimethyl sulfoxide, DMSO) treatment for 3 h. Fold changes of the immunoblot band intensities are shown (middle and right). *P0.05, **P0.01, ***P0.001; Student’s t-test, n=3. (e) Sections of the liver and muscle tissues from fasted 12-week-old GFP-LC3+-Atg7+/+ and GFP-LC3+-Atg7+/− mice were subjected to fluorescent microscopy to examine GFP-LC3 puncta (left). The number of GFP-LC3 puncta was counted (right). Scale bars, 10 μm. *P0.05; Student’s t-test, n=5. (f) Tissue lysates were prepared from the liver of fasted Atg7+/+ and Atg7+/− mice 4 h after leupeptin administration, and immunoblotting was done. Fold changes of the immunoblot band intensities are shown (right). *P0.05; Student’s t-test, n=3.
Systemic autophagy insufficiency compromises adaptation to metabolic stress and facilitates progression from obesity to diabetes (2014)
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(a) Non-fasting blood glucose level was monitored weekly in Atg7+/+, Atg7+/−, Atg7+/+-ob/ob and Atg7+/−-ob/ob mice. ***P0.001; two-way ANOVA. (b) IPGTT was done by glucose injection at 16 weeks of age as described in the Methods (left), and AUC calculated (right). *P0.05, **P0.01, ***P0.001; Student’s t-test (left) and one-way ANOVA (right). (c) HOMA-IR index was calculated as described in Methods. *P0.05; one-way ANOVA. (d) ITT was performed by insulin injection at 16 weeks of age as described in the Methods. *P0.05, **P0.01, ***P0.001; Student’s t-test. (e) Tissue lysates from Atg7+/+-ob/w, Atg7+/−-ob/w, Atg7+/+-ob/ob and Atg7+/−-ob/ob mice were prepared before and 7 min after injection of 5 U kg−1 regular insulin (Ins) into the tail vein, and subjected to immunoblot analysis using antibodies specific for phospho-Akt S473 and total Akt. Numbers below immunoblot bands indicate the fold changes normalized to control bands.
Systemic autophagy insufficiency compromises adaptation to metabolic stress and facilitates progression from obesity to diabetes (2014)
f3

(a) Tissue lysates from each type of mouse were subjected to immunoblot analysis using antibodies specific for total JNK, phospho-JNK, total IRS-1 and phospho-IRS-1 S307. (b) Liver sections from each type of mouse were subjected to immunohistochemistry using anti-nitrotyrosine antibody. Scale bars, 100 μm. (c) Tissue lysates were prepared from 18-week-old mice of each genotype, and subjected to immunoblot analysis using a kit detecting carbonylated proteins. (d) Immunoblot analysis was performed using anti-phospho-p53 and -p53 antibodies. p21 and β-actin mRNA expression was evaluated by RT–PCR. Numbers below immunoblot bands indicate the fold changes normalized to control bands.
Systemic autophagy insufficiency compromises adaptation to metabolic stress and facilitates progression from obesity to diabetes (2014)
f4

(a) GFP-LC3 puncta were visualized by fluorescent microscopy of tissue from each type of mouse in fed state, and the numbers of GFP-LC3 puncta counted. Scale bars, 20 μm. *P0.05, **P0.01; Student’s t-test. (b) Tissues of ob/w and ob/ob mice were subjected to EM, and the number of autophagosomes was counted. ***P0.001; Student’s t-test. (c) Immunoblotting using anti-GFP or -p62 antibody. (d) Tissue lysates were prepared from the liver of fed ob/w or ob/ob mice 4 h after leupeptin administration, and immunoblotting was performed. Numbers below immunoblot bands indicate the fold changes normalized to control bands. (e) After labelling SK-Hep1 cells with C14-leucine, cells were treated with FFAs (600 μM PA or 1,200 μM OA). Percent release of radioactivity was measured for 3–6 h as described in the Methods. The difference between the percent proteolysis without E64d/pepstatin A/NH4Cl and that with E64d/pepstatin A/NH4Cl was regarded as lysosomal proteolysis. *P0.05, **P0.01; one-way ANOVA, n=3. (f) Atg7+/+ and Atg7+/− primary MEFs were loaded with a mixture of the indicated concentrations of PA and OA for 48 h, and TG content was estimated by ORO staining. **P0.01, ***P0.001; two-way ANOVA, n=4. Numbers below immunoblot bands indicate the fold changes normalized to control bands.
Systemic autophagy insufficiency compromises adaptation to metabolic stress and facilitates progression from obesity to diabetes (2014)
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(a) The number of CLSs was counted in WAT of each type of mouse as described in the Methods. *P0.05; one-way ANOVA, n=3. (b) Total mRNA was extracted from each tissue, and RT–PCR was done using primers specific for Tnfa, Il6, F4/80 or pro-Il1b. The expression of pro-Il1b was determined using SVF fraction of WAT tissue. (c,d) Lysate of SVF was subjected to immunoblot analysis using anti-IL-1β (c) or anti-caspase-1 antibody (d). (e) Primary peritoneal macrophages were isolated, and treated with PA of the indicated concentrations in the presence or absence of LPS. ELISA was conducted to determine IL-1β concentrations in the culture supernatant. (BSA, bovine serum albumin) ***P0.001; two-way ANOVA, n=4. (f) After incubation of primary peritoneal macrophages with PA of the indicated concentrations with or without LPS for 16 h, NAD+/NADH ratio was determined using a commercial kit. *P0.05, **P0.01, ***P0.001; two-way ANOVA, n=5. (g) After the same treatment of peritoneal macrophages as in f, cells were incubated with MitoSOX to measure mitochondrial ROS by fluorescence-activated cell sorting (FACS) analysis. (h) After the same treatment of peritoneal macrophages as in f, cells were stained with MitoTracker Red and MitoTracker Green for FACS analysis to determine mitochondrial potential. The numbers in g,h indicate the percentages of cells in the designated gate. Numbers below immunoblot bands indicate the fold changes normalized to control bands.
Systemic autophagy insufficiency compromises adaptation to metabolic stress and facilitates progression from obesity to diabetes (2014)
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(a) Atg7+/− and control Atg7+/+ mice were fed HFD or normal chow diet (NCD), and non-fasting blood glucose levels were monitored. *P0.05, **P0.01; Student’s t-test. (b) Fasting blood glucose levels were determined after 18 weeks of HFD. *P0.05; one-way ANOVA. (c) IPGTT was performed after 18 weeks of HFD, (left) and AUC calculated (right). *P0.05; Student’s t-test (left) and one-way ANOVA (right). (d) HOMA-IR was calculated after 18 weeks of HFD. ***P0.001; one-way ANOVA. (e) ITT was performed after 18 weeks of HFD (left), and KITT calculated (right). *P0.05; Student’s t-test (left) and one-way ANOVA (right).
PICALM modulates autophagy activity and tau accumulation (2014)
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(a) Western blot analysis of CALM, actin, GAPDH and LC3-II in several cell lines
(HeLa, HEK, CAD and murine embryonic fibroblast (MEF)) where CALM was knocked down using shRNA
or siRNA, as indicated, or knockout with rescue experiment. In all
experiments in this paper, we used a scramble siRNA or a luciferase shRNA as
controls. The cells were starved in Hanks balanced salt solution (HBSS) and
treated with Baf A1 as
indicated. (BC, basal conditions; SE, short exposure; LE, longer exposure).
Quantification of LC3-II/actin or GAPDH ratio is shown in Supplementary Fig. 1A. *Not specific.
(b) LC3 dot counting in CALM knockdown cells. CALM was knocked down in HeLa cells
expressing GFP-LC3 and with or without an siRNA-resistant form of wild-type
CALM (rescue), as
indicated. The cells were starved in HBSS for 4 h, fixed and
subjected to microscopy to score the number of LC3 dots per cell. The
knockdown efficiency and the level of the siRNA-resistant form of
CALM are shown on the
left on the western blotting. The number of LC3 dots per cell (shown as mean
±s.d.) is shown on the graph for each condition
(n≥300 cells per condition; BC, basal conditions). The
ratio of the number of LC3 dots per cell between starvation and basal
conditions is shown on the right (*P0.01; NS, not
significant, two-tailed t-test). Pictures obtained from automated
microscope are shown. Scale bars, 20 μm.
PICALM modulates autophagy activity and tau accumulation (2014)
f2

(a) p62 vesicle
formation in CALM
knockdown HeLa cells. Confocal pictures are shown. #CALM-downregulated cells where
p62 vesicles
accumulate. Data are representative of three independent experiments and
shown as mean ±s.e.m. (n≥500 cells;
*P0.01; two-tailed t-test). Scale bars,
5 μm. (b) Western blot analysis of p62, actin and GAPDH in HeLa cells
and HEK cells (basal conditions, BC, or without serum for 1 h)
where CALM was knocked
down using shRNA or siRNA, as indicated. Data are mean ±s.d
(n=3 experiments for HeLa cells and HEK cells;
*P0.05; two-tailed t-test). (c) Percentage of
Q74-expressing cells with aggregates in CALM knockdown HeLa cells. Data depict one
representative experiments performed in triplicate, out of three independent
experiments and shown as mean ±s.d. (*P0.05;
two-tailed t-test). (d) Tau-positive tangle formation in CALM knockdown cells. HeLa cells
transiently expressing DsRed-tau 4R were treated with Baf A1 for 4 h as
indicated. Cells were fixed and analysed by confocal microscopy after
immnunostaining for phosphorylated tau using PHF1 antibody (green). Data represent the
number of cells with phosphorylated tau-positive tangles as mean ±s.e.m.
(n=3 experiments; *P0.01; two-tailed t-test).
Scale bars, 5 μm.
PICALM modulates autophagy activity and tau accumulation (2014)
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(a) Formation of endogenous ATG12 vesicles in CALM knockdown HeLa cells in basal (BC) and serum
starvation conditions. Confocal pictures are shown with arrows indicating
ATG12 vesicles in
starvation conditions. Data are from one representative experiment, out of
three independent experiments. Data shown as mean ±s.e.m.
(n≥500 cells; *P0.01; two-tailed
t-test). Scale bars, 5 μm. (b)
Co-localization between GFP-ATG16L1 and internalized cholera toxin subunit B conjugated
with Alexa555 (CTX; 20 min) in CALM knockdown HeLa cells. Confocal
pictures are presented with magnified areas showing the co-localization
between ATG16L1 and CTX
in greater detail. Scale bars, 5 μm. The
Pearson’s coefficient between ATG16L1 and cholera toxin is shown. Data are
representative of three independent experiments and shown as mean
±s.d. (n≥20 cells; *P0.05;
two-tailed t-test). (c) Size of endogenous ATG12 vesicles in CALM knockdown HeLa cells in
starvation conditions. Confocal pictures are shown with arrows indicating
ATG12 vesicles and #
indicating CALM knockdown
cells. Data are representative of three independent experiments and shown as
mean ±s.d. (n≥100 vesicles;
*P0.05; two-tailed t-test). (AU, arbitrary unit).
Scale bars, 5 μm. (d) Live-cell imaging of
ATG16L1-GFP in
CALM knockdown HeLa
cells. Confocal pictures from various time points of a 5-min movie are shown
in inverted grey style. Arrows indicate ATG16L1 vesicles. The number of fusion events per
5 min is shown. Data are representative of five movies and shown
as mean ±s.d. (*P0.05; two-tailed t-test).
Scale bars, 5 μm. (e) In vitro fusion
assay of post-nuclear supernatant from HeLa cells expressing either
GFP-ATG16L1 or
mStrawberry-ATG16L1
in control and CALM
knockdown conditions. Confocal pictures are shown where ATG16L1-mStrawberry signal is shown
in purple to enable better visualization. Fused vesicles appear in white.
The ATP-negative
condition, which prevents SNARE-dependent fusion, is also shown as a control
for the reaction. Magnified areas are shown to allow visualization of the
vesicles. The percentage of fused vesicles is represented. n=numbers
of vesicles scored per field (a minimum of five fields were analysed per
condition). Data are representative of two independent experiments and shown
as mean ±s.d. (n≥100 vesicles). Scale bars,
5 μm. (*P0.05; two-tailed
t-test).
PICALM modulates autophagy activity and tau accumulation (2014)
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(a) LC3 levels in CALM knockdown cells. CALM was knocked down in cells
expressing or not expressing an siRNA-resistant form of CALM wild type (wt) or
CALM 219 mutant, as
indicated. The cells were lysed and subjected to western blotting. The
knockdown efficiency, LC3-II levels and the level of the siRNA-resistant
form of CALM are shown on
the western blotting. (b) LC3 dots counting in CALM knockdown cells. CALM was knocked down in cells
expressing GFP-LC3 with or without an siRNA-resistant form of CALM wild type (wt) or
CALM mutant (219
mutant) as indicated. The cells were kept in full medium or starved in Hanks
balanced salt solution (HBSS) for 4 h, fixed and subjected to
microscopy to score the number of LC3 dots per cell. The ratio of the number
of LC3 dots per cell (shown as mean ±s.d.) between starvation and
basal conditions is shown on the graph (*P0.01; NS, not
significant, two-tailed t-test; n≥300 cells per
condition; BC, basal conditions). (c) Co-localization between
ATG9A and
VAMP3-HA or GFP-LC3
and VAMP8-HA in control
and CALM knockdown HeLa
cells stably expressing VAMP3-HA or VAMP8-HA. Confocal pictures are shown with magnified
areas showing co-localization between ATG9A and VAMP3 or GFP-LC3 and VAMP8 in control cells and no co-localization in
CALM knockdown cells.
Quantification of ATG9A-VAMP3 or GFP-LC3-VAMP8 co-localization is shown on the graph as a
Pearson’s coefficient (data are mean ±s.d.;
*P0.05; two-tailed t-test). Scale bars,
5 μm.
PICALM modulates autophagy activity and tau accumulation (2014)
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(a) Co-localization between ATG12 and VAMP2-HA in control and CALM knockdown HeLa cells stably
expressing VAMP2-HA.
Confocal pictures are shown with magnified areas on the right showing
co-localization between ATG12 and VAMP2 in control cells and no co-localization in
CALM knockdown cells.
Quantification of ATG12-VAMP2 co-localization is shown on the graph as the
Pearson’s coefficient (data are mean
±s.d.;*P0.05; two-tailed t-test). Scale bars,
5 μm. (b) Western blot analysis of VAMP2, actin and LC3-II in HeLa
cells where VAMP2 was
knocked down, as indicated. The cells were starved in Hanks balanced salt
solution (HBSS) and treated with Baf
A1 as indicated. (SE, short exposure; LE, longer
exposure.) Quantification of LC3-II/actin ratio is shown. Data are
representative of three independent experiments and shown as mean
±s.d. (*P0.05; NS, not significant, two-tailed
t-test). (c) LC3 dot counting in CALM and VAMP2 knockdown cells.
CALM or VAMP2 were knocked down in cells
expressing GFP-LC3. The cells were kept in full medium or starved in HBSS
for 4 h, fixed and subjected to automated fluorescence microscopy
to score the number of LC3 dots per cell. The number of LC3 dots per cell
(shown as mean ±s.d.) is shown on the graph for each condition
(n≥300 cells per condition; BC, basal conditions).
(*P0.01; NS, not significant, two-tailed t-test).
(d) Number of p62 dots per cell in VAMP2 knockdown. HeLa cells where VAMP2 was knocked down were fixed
and subjected to microscopy after labelling endogenous p62 using specific antibody. The
data represent the number of p62 dots per cell shown as mean ±s.d.
(*P0.05; two-tailed t-test;
n≥300 cells per condition). (e) Percentage of
Q74-expressing cells with aggregates in VAMP2 knockdown HeLa cells. Data are from one
representative experiments performed in triplicate, out of three independent
experiments and shown as mean ±s.d. (*P0.05;
two-tailed t-test). (f) Western blot analysis of VAMP2, actin and LC3-II in HeLa
cells stably expressing VAMP2-HA wild type or VAMP-2-HA mutated in the
CALM-binding site at
different levels (wild-type clone 6, wt Cl6: low level; wild-type clone 11,
wt Cl11: high level; mutant clone 11, AA Cl11: low level; mutant clone 12,
AA Cl12: high level). The cells were treated with Baf A1 as indicated. (SE, short
exposure; LE, longer exposure). Quantification of LC3-II/actin ratio is
shown. Data are representative of three independent experiments and shown as
mean ±s.d. (*P0.05; two-tailed t-test).
PICALM modulates autophagy activity and tau accumulation (2014)
f6

(a) Size of endogenous ATG12 vesicles in HeLa cells stably expressing either
wild-type or mutant VAMP2. Confocal pictures are presented with magnified areas
showing ATG12 vesicles.
Data are representative of three independent experiments and shown as mean
±s.d. (n≥100 vesicles; *P0.05; two
tail t-test). Scale bars, 5 μm. (b)
Co-localization between ATG12 and LC3 in HeLa cells stably expressing either
wild-type clone 11 or mutant clone 12 VAMP2. Confocal pictures are presented with magnified
areas showing ATG12-LC3
co-localization. The Pearson’s coefficient between ATG12 and LC3 is shown. Data are
representative of three independent experiments and shown as mean
±s.d. (n≥100 vesicles; *P0.05;
two-tailed t-test). Scale bars, 5 μm. (c)
Size and number of endogenous ATG12 vesicles in VAMP2-knockdown HeLa cells in starvation condition.
Confocal pictures are shown with arrows indicating ATG12 vesicles. Data are
representative of three independent experiments and shown as mean
±s.d. for the size of ATG12 vesicle. (n≥100 vesicles;
*P0.05; based two-tailed t-test). Scale bars,
5 μm. (d) Live-cell imaging of ATG16L1-GFP in VAMP2-knockdown HeLa cells.
Confocal pictures from various time points of a 5-min movie are shown in
inverted greyscale. Arrows indicate ATG16L1 vesicles. The number of fusion events per
5 min is shown. Data are representative of five movies and shown
as mean ±s.d. (*P0.05; two-tailed t-test).
Scale bars, 5 μm. (e) In vitro fusion
assay of post-nuclear supernatants from control and VAMP2 knockdown HeLa cells
expressing either GFP-ATG16L1 or mStrawberry-ATG16L1. Confocal pictures are
shown where ATG16L1-mStrawberry signal is shown in purple to enable
better visualization. Fused vesicles appear in white. The ATP-negative condition, which
prevents SNARE-dependent fusion, is also shown as a control of reaction.
Magnified areas are shown to allow visualization of the vesicles. The
percentage of fused vesicles (white) is represented. Data are representative
of two independent experiments and shown as mean ±s.d.
(n≥100 vesicles). Scale bars, 5 μm.
(*P0.05; two-tailed t-test). n=numbers of
vesicles scored per field.
PICALM modulates autophagy activity and tau accumulation (2014)
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(a) Western blotting showing downregulation of lap (i) or increase in
Atg8a-II (ii)
expression level in adult fly heads on lap downregulation using
the UAS-RNAi lines lapGD12732 or
lapKK105767, or the
heterozygous allele lap1. Quantification of
lap/actin and
Atg8a-II/actin is
shown. Genotypes: Control w; elav-GAL4/+; for the RNAi lines:
w;
elav-GAL4/
lapKK105767 and
w;
elav-GAL4/+;
lapGD12732/+; for
the lap1 allele:
w;
elav-GAL4/+;
lap1/+. (b)
Western blotting showing the accumulation of tau in Drosophila adult fly
heads on lap
downregulation using the UAS-RNAi lines lapGD12732 or lapKK105767, or the
heterozygous allele lap1. Quantification of
tau/actin is shown.
Genotypes: Control w;
elav-GAL4/+;
for tau-WT:
w;
elav-GAL4/+;
UAS-tau-WT/+; for RNAi lines: w; elav-GAL4/ lapKK105767;
UAS-tau-WT/+
and w; elav-GAL4/+;
lapGD12732/tau-WT; for the
lap1 allele:
w;
elav-GAL4/+;
lap1/+ or
w;
elav-GAL4/+;
lap1/UAS-tau-WT.