EMBO/soda-nel huggingface dataset:
Notch and EGFR regulate apoptosis in progenitor cells to ensure gut homeostasis in Drosophila (2019)
Figure 4

Figure 4. Tuneable apoptosis through tuneable Diap1 signals

(A) A model of the regulation of physiological cell death in EC-committed EBs based on our epistatic analysis and previous known gene interactions.

(B and B') Number of ECs over time (left), number of EBs over time (middle), and probabilities of EB loss through apoptosis (right graph). The simulation starts with 1000 EC cells in all figures (Supplementary material and methods; Appendix Table S1). In (B) a challenge at day 1 imposes a loss of 500 EC cells (black dashed vertical line). In (B') two successive challenges are imposed: one at day 1, reducing by half the number of ECs (as in B), and a second one at day 3, causing a loss of 200 cells.

(C) All EBs show Diap1-GFP expression but at varying levels, consistent with EB death fate being tuned by apoptotic input counteracting survival signals.

(D) Quantification of the number of Diap1-GFP+. Note that in p35-expressing midguts reared in 'Low', GFP levels are not increased, consistent with the p35 protein suppressing apoptosis downstream of Diap1.

(E) Quantification of the number of newly renewed ECs in the indicated genotypes after 7 days Increase in EB numbers and EC turnover in the EGFRact midgut reflects both suppression of EB deaths and the non-autonomous stimulation of ISC in this background.

(F) Representative images acquired using the same laser intensity are shown for Diap1-GFP in the indicated illustrative examples. Scale bar, 100µm.

Data information: (C-E) (n= 17, 13, 12, 10, 21, 24). P values were calculated using one-way ANOVA Bonferroni corrected (****, P < 0,0001).

Expanded View Figure legends
In vitro and in vivo drug screens of tumor cells identify novel therapies for high-risk child cancer (2021)
Figure 3

Figure 3. In vivo drug efficacy studies in patient derived xenografts.

A Treatment response in 16 hematologic malignancy (HM) and non-CNS solid PDX models. Objective responses including maintained complete response (MCR), complete response (CR) and partial response (PR) were observed in 10 of 16 models. Drugs are indicated as chemotherapy (Ch), targeted agent (T) or combination treatment (C).

B-D Event-free survival (EFS) and percentage of human CD45+ leukocytes in peripheral blood in 3 acute lymphoblastic leukemia (ALL) orthotopic models.

E-K EFS and tumor volume in 7 non-CNS subcutaneous PDX models which demonstrated objective response in 1 or more treatments.

L EFS in a CNS orthotopic model in which drug sensitivity was observed. EFS is time of inoculation of tumor cells to event (defined by neurologic symptoms or weight loss).

Survival curves were estimated for each treatment group using the Kaplan-Meier method and compared with the untreated control group in each PDX model statistically using log rank test. P value for EFS: ns, not significant; * P<0.05; ** P<0.01; *** P<0.001. The exact P values are provided in Appendix Table S6. ALCL, anaplastic large cell lymphoma; CYCLO, cyclophosphamide; IRN, irinotecan; PD, progressive disease; SD, stable disease; TOPO, topotecan; TMZ, temozolomide; VXL, vincristine/dexamethasone/L-asparaginase.
eEF2 in the prefrontal cortex promotes excitatory synaptic transmission and social novelty behavior (2022)
Figure 1

Figure 1. eEF2 is highly expressed in the excitatory neurons in mouse brain.

A Western blots of eEF2 expression in different brain regions, GAPDH was used as a loading control.

B eEF2 expression levels were quantified and represented as fold changes of that in the hippocampus. n=3 mice for each brain region.

C Immunofluorescent staining of eEF2 (green) and different nervous system cells (red: NeuN/GFAP/IBA1/OLIG2/CaMKⅡα/GAD65/67) in somatosensory cortex of adult mice brains. Arrows indicate highly colocalized cells. Scale bar, 10 μm.

D, E Colocalization of eEF2 and each cellular marker was quantified by calculating the Manders' Colocalization Coefficients. 6 slices from 3 mice in each condition. (D) One-way ANOVA with Bonferroni's multiple comparisons post hoc, ****p<0.0001 (NeuN+/eEF2+ versus GFAP+/eEF2+), ****p<0.0001 (NeuN+/eEF2+ versus IBA1+/eEF2+), ****p<0.0001 (NeuN+/eEF2+ versus OLIG2+/eEF2+). (E) Unpaired t test, **p=0.0065 (CaMKⅡα+/eEF2+ versus GAD65/67+/eEF2+).

Data information: All data are shown as means ± s.e.m. All the t tests are two-tailed.
eEF2 in the prefrontal cortex promotes excitatory synaptic transmission and social novelty behavior (2022)
Figure 2

Figure 2. Reduced eEF2 protein level and decreased protein synthesis in excitatory neurons of the prefrontal cortex in Eef2 HET mice.

A A schematic showing the CRISPR/Cas9 strategy used to delete Eef2.

B Western blots of eEF2 in the PFC, the rest part of cortex, the hippocampus, and the striatum of Eef2 WT and HET mice.

C Quantification analysis of (B). n=5 mice for cortex (without PFC), n=8 mice for PFC, n=9 mice for HP, n=3 mice for striatum. Unpaired t tests. Cortex (without PFC), p=0.9757; PFC, **p=0.0049; HP, p=0.1338; Striatum, p=0.7301.

D Representative merged immunofluorescent staining images of eEF2 (green) and CaMKⅡα (red) in the mPFC of Eef2 WT and HET mice. Scale bar, 10 μm.

E Quantification of mean fluorescent intensity of eEF2 in CaMKⅡα+ cells in WT and HET mPFC. n=918 cells from 3 WT mice, n=965 cells from 3 HET mice. Unpaired t test. **** p<0.0001.

F Representative merged immunofluorescent staining images of eEF2 (green) and GAD65/67 (red) in the mPFC of Eef2 WT and HET mice. Scale bar, 10 μm.

G Quantification of mean fluorescent intensity of eEF2 in GAD65/67+ cells in WT and HET mPFC. n=690 cells from 3 WT mice, n=686 cells from 3 HET mice. Mann-Whitney test. p=0.6757.

H Western blots of de novo global protein synthesis in PFC slices of WT and HET mice, measured by SUnSET. α-tubulin was used as a loading control.

I Quantification analysis of puromycin-labeled protein levels. WT, n=5 mice, HET, n=4 mice. Unpaired t tests. **p=0.0011.

J Representative images of AHA incorporation (green) with CaMKⅡα+ staining (red) in mPFC of WT and HET mice. Arrows indicate CaMKⅡα+ cells. Scale bar, 20 μm.

K Quantification of total AHA incorporation. 12 slices from 3 mice for each genotype. Unpaired t test. *p=0.0268.

L Quantification of AHA incorporation in CaMKⅡα+ cells. WT, n=276 cells from 3 WT mice, n=293 cells from 3 HET mice. Mann-Whitney test. **** p<0.0001.

Data information: All data are shown as means ± s.e.m. All the tests are two-tailed.
eEF2 in the prefrontal cortex promotes excitatory synaptic transmission and social novelty behavior (2022)
Figure 3

Figure 3. Altered proteome and reduced number of excitatory synapses in the prefrontal cortex of Eef2 HET mice.

A PFC, indicated by the boxed area, was examined for LC-MS/MS for synaptosome proteome.

B Principal component analysis (PCA) of all quantified data sets of PFC synaptosome proteome. Green triangles and orange circles represent WT and HET samples, respectively.

C A heatmap of expression levels of top 15% altered proteins in all samples.

D, E Gene ontology (GO) enrichment analysis for top 15% altered proteins of WT and HET samples. Bubble charts showed main biological process (BP) and molecular function (MF) terms with significant enrichment (p value < 0.05, FDR < 0.25) from down-regulated (D) and up-regulated (E) proteins.

F Gene Set Enrichment Analysis (GSEA) was performed to analyze expression cohorts from WT and HET PFC synaptosome. Enrichment plots of the GO Mitochondrial Translation gene set (NES=−1.56, FDR=0.010), Actin Binding gene set (NES=−1.28, FDR=0.023) and Cell Adhesion gene set (NES=−1.20, FDR=0.080) were shown. NES, normalized enrichment score.

G Representative images of Golgi‐stained dendrite spines in the mPFC from WT and HET mice. Scale bar, 5 μm.

H Quantification of spine density per 10 μm of dendrites. n=18 dendrites from 3 WT mice; n=23 dendrites from 3 HET mice. Unpaired t test. ****p<0.0001.

I Representative Western blots of expression levels of AMPAR and NMDAR subunits in the synaptosomal fraction of WT and HET PFC. α-tubulin was served as a loading control.

J Quantification analysis of synaptosomal expression of different receptor subunits. Unpaired t test. GluA1, p=0.9346; GluA2, **p=0.0075; GluN1, p=0.6946; GluN2A, p=0.4091; GluN2B, p=0.0796. n.s., not significant. n=5 mice for each genotype.

K The schematic of puromycin-proximity ligation assay (PLA).

L Representative immunofluorescent images of eEF2 (magenta) and PLA signals (white) in lentivirus (LV)-scramble-EGFP or LV-Eef2 shRNA-EGFP infected primary cortical neurons (green, DIV 14). Scale bar, 10 μm.

M Quantification of mean fluorescent intensity of eEF2 in EGFP+ cells in scramble and Eef2 shRNA groups. 64 cells for scramble group and 51 cells for Eef2 shRNA group from 3 independent experiments. Mann-Whitney test. ****p<0.0001.

N Quantification of mean fluorescent intensity of PLA signals in EGFP+ cells in the two groups. The PLA signals represent newly synthesized GluA2. 64 cells for scramble group, 51 cells for Eef2 shRNA group from 3 independent experiments. Mann-Whitney test. ****p<0.0001.

Data information: All data are shown as means ± s.e.m. All the tests are two-tailed.
WDR63 inhibits Arp2/3-dependent actin polymerization and mediates the function of p53 in suppressing metastasis (2020)
Figure 1

Figure 1. WDR63 inhibits cell migration, invasion, and metastasis.

(A and B) A549 cells expressing control shRNA, WDR63 shRNA#1, WDR63 shRNA#2, PCDH control, or PCDH-Flag-WDR63 were subjected to wound-healing (A) and transwell migration (B) assays. The shown images are representative of three independent experiments. Data shown are mean ± SD (n=3). **, P ˂ 0.01; ***, P ˂ 0.001; One-way ANOVA. Scale bar in (A): 200 μm. Scale bar in (B): 100 μm. The successful knockdown and overexpression of WDR63 are shown in Fig EV1C.

(C) Effect of WDR63 knockdown on the migration of A549 cells was analyzed by single cell tracking with time-lapse microscopy at 10 min intervals for 4 h. Scale bar: 200 μm. Cell migration speed, persistence, and mean squared displacement (MSD) were also analyzed using an Excel macro described by Gorelik and Gautreau. Data shown are mean ± SD. n = 3 independent experiments. *, P ˂ 0.05; **, P ˂ 0.01; ***, P ˂ 0.001; One-way ANOVA. The knockdown efficiency of WDR63 is shown in Fig EV1G.

(D) A549 cells expressing control shRNA, WDR63 shRNA#1, WDR63 shRNA#2, PCDH control, or PCDH-Flag-WDR63 were subjected to transwell invasion assay. The shown images are representative of three independent experiments. Data shown are mean ± SD (n=3). *, P ˂ 0.05; **, P ˂ 0.01; ***, P ˂ 0.001; One-way ANOVA. Scale bar: 100 μm.

(E-G) A549 cells expressing control shRNA, WDR63 shRNA#1, or WDR63 shRNA#1 plus shRNA-resistant Flag-WDR63 were subjected to transwell migration (E), single cell tracking (F), and transwell invasion (G) assays. The shown images are representative of three independent experiments. Cell migration speed, persistence, and mean squared displacement (MSD) were also analyzed using an Excel macro described by Gorelik and Gautreau. Data shown are mean ± SD. n = 3 independent experiments. *, P ˂ 0.05; **, P ˂ 0.01; ***, P ˂ 0.001; One-way ANOVA. Scale bar in (E and G): 100 μm. Scale bar in (F): 200 μm. The successful knockdown and overexpression of WDR63 are shown in Fig EV1Q.

(H) A549 cells expressing control shRNA, WDR63 shRNA#1, or WDR63 shRNA#2 (each also expressing luciferase) were injected via tail vein into nude mice (n=6 for each group). Three weeks after injection, tumor formation was monitored by bioluminescence imaging. Data shown are mean ± SD; *, P ˂ 0.05; One-way ANOVA.
WDR63 inhibits Arp2/3-dependent actin polymerization and mediates the function of p53 in suppressing metastasis (2020)
Figure 2

Figure 2. WDR63 is a transcriptional target of p53.

(A) WDR63 mRNA and protein levels in A549, H292, and HCT116 cells transduced with empty vector (PCDH) or PCDH-p53. Data shown are mean ± SD; n = 3 independent experiments. **, P ˂ 0.01; ***, P ˂ 0.001; two-tailed Student's t-test.

(B) WDR63 mRNA and protein levels in A549, H292, and HCT116 cells transduced with control (shctrl) or p53 (shp53) shRNA. Data shown are mean ± SD; n = 3 independent experiments. ***, P ˂ 0.001; two-tailed Student's t-test.

(C) A549 cells expressing control or p53 shRNA were treated with doxorubicin (Dox, 1μg/ml) for the indicated periods of time. WDR63 mRNA and protein levels were then examined. Data shown are mean ± SD; n = 3 independent experiments. ***, P ˂ 0.001; two-tailed Student's t-test.

(D) WDR63 mRNA levels in H1299 cells transfected with empty vector (-), wild-type p53, or the indicated p53 mutants. Data shown are mean ± SD; n = 3 independent experiments. ***, P ˂ 0.001; two-tailed Student's t-test.

(E) Schematic illustration of the first two exons of WDR63 gene. BS1 and BS2 represent 2 putative p53 binding sites predicted by the JASPAR database. Black bars represent p53 binding sites identified in the indicated p53 ChIP-seq datasets. The pGL3-based wild-type and mutant reporter constructs used for luciferase assay are also shown.

(F) Lysates from A549 cells were subjected to ChIP assay using control IgG or anti-p53 antibody. ChIP products were amplified by real-time PCR. Data shown are mean ± SD; n = 3 independent experiments. ***, P ˂ 0.001; two-tailed Student's t-test.

(G) A549 cells were transfected with empty vector (ctrl) or Flag-p53 plus the indicated reporter constructs. Twenty-four hours later, reporter activity was measured. Data shown are mean ± SD; n = 3 independent experiments. **, P ˂ 0.01; ***, P ˂ 0.001; two-tailed Student's t-test.

(H) A549 cells expressing control or p53 shRNA were transfected with pGL3-BS1 and Renilla luciferase plasmids. Twenty-four hours later, cells were treated with or without Nutlin (10 μM) for another 12 h. Reporter activity was then measured. Data shown are mean ± SD; n = 3 independent experiments. **, P ˂ 0.01; two-tailed Student's t-test.
WDR63 inhibits Arp2/3-dependent actin polymerization and mediates the function of p53 in suppressing metastasis (2020)
Figure 3

Figure 3. WDR63 interacts with the Arp2/3 complex.

(A) A ~44 kD protein band specifically pulled down by GST-WDR63 from A549 cell lysates was identified as Arp2 by mass spectrometry analysis. The Arp2 peptide sequences obtained by MS are shown.

(B) Lysates from HEK293T cells expressing HA-Arp2 alone or together with Flag-WDR63 were immunoprecipitated by anti-Flag antibody, followed by western blot analysis. Data shown represent three independent experiments.

(C) Lysates from HEK293T cells expressing GFP-WDR63 alone or together with Flag-Arp2 were immunoprecipitated by anti-Flag antibody, followed by western blot analysis. Data shown represent three independent experiments.

(D) Lysates from A549 cells were immunoprecipitated with control IgG or anti-WDR63 antibody, followed by western blot analysis. Data shown represent three independent experiments.

(E) Purified GST or GST-Arp2 proteins immobilized on glutathione beads were incubated with purified Flag-WDR63. Input and bead-bound proteins were analyzed by western blot. Data shown represent three independent experiments.

(F) Purified GST or GST-WDR63 proteins immobilized on glutathione beads were incubated with purified Arp2. Input and bead-bound proteins were analyzed by western blot. Data shown represent three independent experiments.

(G) Lysates from HEK293T cells expressing GFP-WDR63 alone or together with the indicated Flag-tagged each single subunit of the Arp2/3 complex were immunoprecipitated with anti-Flag antibody, followed by western blot analysis. Data shown represent three independent experiments.

(H) Purified Flag-tagged full-length or the indicated truncated WDR63 proteins immobilized on anti-Flag M2 beads were incubated with the purified Arp2/3 complex (Cytoskeleton, Inc.) in vitro. Input and beads-bound proteins were analyzed by western blot. Data shown represent three independent experiments.
WDR63 inhibits Arp2/3-dependent actin polymerization and mediates the function of p53 in suppressing metastasis (2020)
Figure 4

Figure 4. WDR63 suppresses Arp2/3-mediated actin polymerization.

(A) Immunolocalization of Arp2 in a wound-healing assay. A549 cells expressing control or WDR63 were serum-starved for 6 h before they were scratched. Cells were then treated with or without 10% FBS for 30 min, followed by immunofluorescence assay. The branched actin networks were shown by immunostaining with anti-Cortactin antibody. Data shown represent three independent experiments. Scale bar: 20 μm. The lamellipodia formation was quantified by measuring the length of the outer margin of lamellipodia in individual cell (n=20 for each condition), and expressed as the proportion of the total length of the cell perimeter. Data shown are mean ± SD; n = 3 independent experiments. ***, P ˂ 0.001; One-way ANOVA.

(B and C) Effects of full-length WDR63 (B) and WDR63 (1-200) (C) on Arp2/3-mediated actin polymerization were examined by pyrene actin polymerization assays. Various concentrations of WDR63 (B) or WDR63 (1-200) (C) were incubated with 2 μM actin (50% pyrene-labeled), 10 nM Arp2/3 and 400 nM GST-VCA as indicated. Data shown represent three independent experiments.

(D) Effect of WDR63 on Arp2/3-mediated branched actin polymerization was analyzed by electron microscopy. 0.6 μM WDR63 was incubated with 2 μM actin, 10 nM Arp2/3 and 400 nM GST-VCA as indicated. Actin structures were then stabilized with addition of 2μM phalloidin, followed by electron microscopy analysis. The arrows indicate actin branch junctions. The percentage of branched actin filaments was expressed as the ratio of the number of actin filaments with branch junctions to the total numbers of actin filaments. For each condition, over 150 actin filaments were counted. Data shown are mean ± SD; n = 3 independent experiments. ***, P ˂ 0.001; two-tailed Student's t-test. Scale bar: 200 nm.

(E and F) Increasing amounts of purified Flag-WDR63 (0.1 μM, 0.2 μM, and 0.4 μM) (E) or Flag-WDR63 (1-200) (0.25 μM, 0.5 μM, and 1 μM) (F) was incubated with the Arp2/3 complex (10 nM) and GST-VCA as indicated in vitro, followed by GST pull-down assay. Data shown represent three independent experiments.
WDR63 inhibits Arp2/3-dependent actin polymerization and mediates the function of p53 in suppressing metastasis (2020)
Figure 5

Figure 5. WDR63 inhibits cell migration and invasion through the Arp2/3 complex.

(A-D) A549 cells expressing control shRNA, WDR63 shRNA#1, Arp2 shRNA, or both WDR63 and Arp2 shRNA were subjected to wound-healing (A), transwell migration (C) and transwell invasion (D) assays. Lysates from these cells were also analyzed by western blot (B). The shown images are representative of three independent experiments. Data shown are mean ± SD (n=3). *, P ˂ 0.05; ***, P ˂ 0.001; N.S., no significance; One-way ANOVA. Scale bar in (A): 200 μm. Scale bars in (C and D): 100 μm.

(E-G) A549 cells expressing either control shRNA or WDR63 shRNA#1 were infected with lentiviruses expressing Flag-tagged full-length or truncated WDR63 proteins as indicated. Cells were then subjected to transwell migration (E) and transwell invasion (G) assays. Lysates from these cells were also analyzed by western blot (F). The shown images are representative of three independent experiments. Data shown are mean ± SD (n=3). *, P ˂ 0.05; **, P ˂ 0.01; ***, P ˂ 0.001; One-way ANOVA. Scale bar: 100 μm.
WDR63 inhibits Arp2/3-dependent actin polymerization and mediates the function of p53 in suppressing metastasis (2020)
Figure 6

Figure 6. WDR63 mediates p53's function in suppressing cell migration, invasion and metastasis.

(A-D) A549 cells expressing control shRNA, p53 shRNA, or p53 shRNA plus Flag-WDR63 were subjected to wound-healing (A), transwell migration (C) and transwell invasion (D) assays. Lysates from these cells were also analyzed by western blot (B). The shown images are representative of three independent experiments. Data shown are mean ± SD (n=3). **, P ˂ 0.01; ***, P ˂ 0.001; One-way ANOVA. Scale bar in (A): 200 μm. Scale bars in (C and D): 100 μm.

(E and F) A549 cells expressing either control shRNA or p53 shRNA were infected with lentiviruses expressing Flag-tagged full-length or truncated WDR63 proteins as indicated. Cells were then subjected to transwell migration (E) and transwell invasion (F) assays. The shown images are representative of three independent experiments. Data shown are mean ± SD (n=3). *, P ˂ 0.05; ***, P ˂ 0.001; One-way ANOVA. Scale bar: 100 μm. The successful knockdown of p53 and overexpression of WDR63 proteins are shown in Fig EV5F.

(G) A549 cells expressing control shRNA, p53 shRNA, or p53 shRNA plus Flag-WDR63 (each also expressing luciferase) were injected via tail vein into nude mice (n=6 for each group). Three weeks after injection, tumor formation was monitored by bioluminescence imaging. Data shown are mean ± SD; *, P ˂ 0.05; One-way ANOVA.

Legends for EV figures
Inhibition of DPP4 activity in humans establishes its in vivo role in CXCL10 post-translational modification: prospective placebo-controlled clinical studies (2016)
Figure 1

Figure 1. Sitagliptin treatment limits DPP4-mediated N-terminal truncation of CXCL10.

(A) CXCL10 assay characteristics. Standard curves of the short, long and total CXCL10 Simoa assays are shown. For each curve, limit of detection (LOD) defined as blank+3SD, are shown as horizontal lines. The LOD was 1.7pg/ml for long and short CXCL10 assays and 0.22pg/ml for total CXCL10. Standard curves were fitted using the 4 Parameter Logistic non-linear regression model. Samples reporting a signal below the LOD were replaced with 1pg/ml for short and long CXCL10. Plasma from healthy individuals receiving (B) placebo (n=9) or (C) sitagliptin (n=27) were analyzed by Simoa. Blood samples were collected at screening visit (SV) and day 0 (D0) before treatment, at day 3 (D3), day 14 (W2) and day 28 (W4) under treatment and 5 weeks after treatment interruption (W9). (C) Plasma from chronic HCV patients receiving sitagliptin (n=3) were collected before (D0) and weekly during sitagliptin treatment (W1 & W3). Antagonist CXCL103-77 (short CXCL10, in blue), agonist CXCL101-77 (long CXCL10, in red) and total CXCL10 (in black) levels are shown. Each dot represents a donor and bars are at the median. Grey areas highlight the period under placebo or sitagliptin treatment. Statistical analysis of (B) and (C) was performed using non parametric Friedman’s test, ns: non significant, **: P<0.01, ****: P<0.001. For (C), additional size effect analysis was performed and Cohen’s d values are reported. No statistical analysis was performed in (D) due to sample size, nd: non-determined.
Ribosome slowdown triggers codon-mediated mRNA decay independently of ribosome quality control (2021)
Figure 4

Figure 4. Modulation of charged tRNA levels in zebrafish embryos.

(A) AnsB causes asparagine deprivation by converting asparagine to aspartic acid. Mock-injected and AnsB-overexpressing zebrafish embryos at 6 hpf are shown.

(B) Charged tRNA levels in mock-injected and AnsB-overexpressing embryos at 6 hpf. Total and charged tRNAs were measured by qRT-PCR coupled to the OXOPAP assay. The relative charged tRNA level in mock-injected embryos were set to one.

(C) qRT-PCR analysis of Asn AAC and Leu CUG codon tag reporter mRNAs at 6 hpf relative to 2 hpf in mock-injected and AnsB-overexpressing embryos.

(D) Poly(A) tail analysis of Asn AAC codon tag reporter mRNA at 2 and 6 hpf. The developmental stages are shown above as hpf. The lane labeled A0 shows the 3´ UTR fragment without a poly(A) tail.

(E) Quantification of the PAT assay at 6 hpf in (D).

(F) Poly(A) tail analysis of Leu CUG codon tag reporter mRNA at 2 and 6 hpf.

(G) Quantification of the PAT assay at 6 hpf in (F).

Data information: In B and C, bar charts show the average of three independent biological replicates. Error bars show SD. Individual data points are shown as dots. P-values were calculated using two-sided Student's t-test.