EMBO/soda-nel huggingface dataset:
Developmental and Functional Heterogeneity of White Adipocytes within a Single Fat Depot (2018)
Figure 3

Figure 3. Clonal cell line clusters exhibit distinct gene expression profiles and morphology.

(A-C and E-J) Expression of Wt1, leucine rich repeat neuronal 4 (Lrrn4), Uroplakin 3b (Upk3b), Tagln, connective tissue growth factor (Ctgf), Keratin 19 (Krt19), Mx1, caspase 1 (Casp1), and C-X-C Motif Chemokine Ligand 12 (Cxcl12) in Immortomouse clonal cell line clusters as preadipocytes (d0) and during six days of adipogenic differentiation. Data are shown as mean ± SEM of 3-7 cell lines/group. Bars indicate significant differences between groups (p<0.05; paired two-way ANOVA).

(D) Bright-field images of preadipocyte cell lines under standard culture conditions. The photographs were taken at 10x magnification.
Developmental and Functional Heterogeneity of White Adipocytes within a Single Fat Depot (2018)
Figure 5

Figure 5. Primary preadipocyte and adipocyte subtypes exhibit differential gene expression profiles and phenotypic characteristics.

A-I) Expression of Wt1, Lrrn4, Upk3b, Tagln, Ctgf, Krt19, Mx1, Casp1, and Cxcl12 in primary preadipocytes isolated from white adipose tissue of 5-6 month old Wt1-creERT2;Rosa26mT/mG, Tagln-cre;Rosa26mT/mG, and Mx1-cre;Rosa26mT/mG male mice. mGFP and mTomato positive preadipocytes were isolated from the pooled visceral fat depots (perigonadal, perirenal, mesenteric, and pericardial) of Wt1-creERT2;Rosa26mT/mG mice, the pooled subcutaneous fat depots (subcutaneous and scapular white) of Mx1-cre;Rosa26mT/mG, and both the pooled visceral (Tagln-V) and subcutaneous depots (Tagln-S) from Tagln-cre;Rosa26mT/mG mice. Data are shown as mean ± SEM of 4-6 mice/group.

J) Bright-field image of immortalized mGFP and mTomato positive preadipocytes after in vitro adipogenic differentiation. Neutral lipoids were stained with Oil Red O and original photographs were at 10x magnification (left panel). Scale bar = 100 μm.

K) Triglyceride content of immortalized mGFP and mTomato positive preadipocytes after six days of differentiation. Data are shown as mean ± SEM of 5-8 replicates, and the entire experiment was repeated with three independent cell lines.

L) Basal extracellular acidification rate (ECAR) of immortalized mGFP and mTomato positive preadipocytes was determined by calculating the area under the curve (AUC) in basal conditions. The whole experiment was repeated twice. Data are shown as mean ± SEM of 3 cell lines per group.

M) Basal respiration of preadipocytes was of immortalized mGFP and mTomato positive preadipocytes determined by calculating the area under the curve (AUC) during measurements of oxygen consumption rate (OCR). The whole experiment was repeated twice. Data are shown as mean ± SEM of 3 cell lines per group.

N) Ratio of basal oxygen consumption rate (OCR) to basal extracellular acidification rate (ECAR) of immortalized mGFP and mTomato positive preadipocytes. Data are shown as mean ± SEM of 3 cell lines per group.

Data information: Asterisks indicate significant differences between mGFP and corresponding mTomato positive preadipocytes isolated from the same mouse line (p<0.05; paired two-way ANOVA) in all panels. Bars indicate significant differences between mGFP preadipocytes isolated from different mice lines (p<0.05; two-way ANOVA).
Developmental and Functional Heterogeneity of White Adipocytes within a Single Fat Depot (2018)
Figure 6

Figure 6. Preadipocytes subpopulations are distributed in a depot-specific manner in vivo.

A-C) Number of mGFP and mTomato positive preadipocytes isolated by FACS from the indicated white adipose depots from 5-6 month old male Wt1-creERT2;Rosa26mT/mG, Tagln-cre;Rosa26mT/mG, and Mx1-cre;Rosa26mT/mG mice. Data are shown as mean ± SEM of 4-9 mice.
Developmental and Functional Heterogeneity of White Adipocytes within a Single Fat Depot (2018)
Figure 7

Figure 7. Adipocyte subpopulations are distributed in a depot-specific manner in vivo.

A) Representative images of whole-mount preparations of the indicated white adipose tissue depots of 5-6 month old Wt1-creERT2;Rosa26mT/mG, Tagln-cre;Rosa26mT/mG, and Mx1-cre;Rosa26mT/mG male mice. The photographs were taken at 10x magnification. Scale bar = 100 μm.

B-D) Quantitation of mGFP and mTomato positive adipocytes from each of the indicated white adipose depots from 5-6 month old male Wt1-creERT2;Rosa26mT/mG, Tagln-cre;Rosa26mT/mG, and Mx1-cre;Rosa26mT/mG mice. Adipocytes were counted from four non-overlapping images per depot per mouse. Data are shown as mean ± SEM of 4-9 mice.
Developmental and Functional Heterogeneity of White Adipocytes within a Single Fat Depot (2018)
Figure 8

Figure 8. Distribution analysis of adipocyte subpopulations within adipose tissue depots

A, B) Number of mGFP positive preadipocytes isolated by FACS from each of the indicated white adipose depots from 5-6 month-old Wt1-creERT2, Tagln-cre, and Mx1-cre crossed to Rosa26mT/mG mice from the experiment shown in Figure 6B. Data are shown as mean ± SEM of 4-9 mice.

C, D) Number of mGFP positive adipocytes from each of the indicated white adipose depots from 5-6 month-old Wt1-creERT2, Tagln-cre, and Mx1-cre crossed to Rosa26mT/mG mice. Four separate non-overlapping images/depot/mouse from the experiment shown in Figure 6C. Data are shown as mean ± SEM of 4-9 mice.

E) Model of Adipose tissue heterogeneous within a single fat depot. Each adipose tissue depot is comprised of a mix of Type 1-3 and uncharacterized preadipocytes and adipocytes.
Human ZBP1 induces cell death-independent inflammatory signaling via RIPK3 and RIPK1 (2022)
Figure 3

Figure 3 - K63-Ub and M1-Ub facilitate ZBP1 inflammatory signaling

A. Western blot analysis of anti-FLAG (ZBP1) immunoprecipitation from HT29 / TO-ZBP1WT cells treated with 0 or 500 ng/mL Dox for 16 h. Blots are representative of three biological replicates. Immunoprecipitated material was treated or not with USP21 (1 μM) for deubiquitination. Input loaded was 5% for ZBP1 and 1% for co-immunoprecipitants. Asterisk indicates antibody heavy chain signal in IP samples.

B. Enrichment of Ub-conjugates by GST-1xUBA for analysis of ubiquitination status of RIPK1, ZBP1 and RIPK3 in HT29 / TO-ZBP1WT cells treated with 0 or 500 ng/mL Dox for 16h. Blots are representative of at least three biological replicates. After enrichment, samples were treated or not with USP21 (1 μM) for deubiquitination. Asterisk indicates unspecific bands. Arrows indicate RIPK3 signal.

C. Enrichment of Ub-conjugates for analysis of the ubiquitination status of RIPK1 and ZBP1 using GST-1xUBA or linkage-specific SUBs in HT29 / TO-ZBP1WT cells treated with 0 or 500 ng/mL Dox for 16 h. See Fig EV3D for two biological replicates.

D. Enrichment of Ub-conjugates by GST-1xUBA for analysis of ubiquitination status of RIPK1 and ZBP1 in HT29, HT29 / TO-ZBP1WT and HT29 / RIPK1-KO aA3 / TO-ZBP1WT cells treated with 500 ng/mL Dox for 16 h. Blots are representative of four biological replicates. Asterisk indicates antibody background signal.

E. NF-κB activity in HEK293FT / RIPK3-2xFV cells transfected with dual luciferase reporters, ZBP1 or EV, and GFP (Ctrl) or GFP-tagged SUBs as indicated. Luciferase reporter activities were measured 24 h after transfection and normalized to GFP+EV-transfected condition. Data is plotted as mean with S.E.M. (n = 4 biological replicates). One-way ANOVA and Sidak's multiple comparisons tests were used to test for statistical differences between the indicated condition and ZBP1/GFP-transfected condition. **** p < 0.0001. Cell lysates were analyzed by Western blotting to determine expression of ZBP1, GFP or GFP-tagged SUBs and Actin. Blots are representative of three biological replicates.

F, G. NF-κB activity in HEK293FT / RIPK3-2xFV cells transfected with dual luciferase reporters, ZBP1 or EV, and variants of CYLD or OTULIN. Luciferase reporter activities were measured 24 h after transfection and normalized to ZBP1/EV-transfected cells. Data is plotted as mean with S.E.M. Multiple Welch t-tests were used to test for statistical differences between the indicated condition and the ZBP1/EV-transfected condition. (F) n = 4 biological replicates. ** p = 0.0012, ns = not significant (p = 0.2342). (G) n = 3 biological replicates. * p = 0.0137; ns = not significant (p = 0.8374). Cell lysates were analyzed by Western blotting to determine expression of ZBP1, CYLD or OTULIN, and Actin. Blots are representative of (F) four or (G) three biological replicates.
Human ZBP1 induces cell death-independent inflammatory signaling via RIPK3 and RIPK1 (2022)
Figure 4

Figure 4 - cIAP1 and LUBAC facilitate ZBP1-induced inflammatory signaling

A. NF-κB activity in HEK293FT / RIPK3-2xFV cells transfected with siRNA targeting HOIP (siHOIP) or a mismatch sequence (siMM), and 48 h later transfected with dual luciferase reporters and ZBP1 or GFP (control). Luciferase reporter activities were measured 24 h after transfection and normalized to the siMM+ZBP1 samples. Data is plotted as mean with S.E.M. (n = 4 biological replicates). A Welch's t-test was used to test for the statistical difference between indicated conditions. **** p < 0.0001. HOIP knockdown and ZBP1 expression levels were analyzed by Western blotting. Blots are representative of three biological replicates.

B. NF-κB activity in HEK293FT / RIPK3-2xFV cells treated with 0 or 100 nM CpA and transfected with dual luciferase reporters and ZBP1 or EV. Luciferase reporter activities were measured 24 h after transfection and normalized to the 0 nM CpA+ZBP1 sample. Data is plotted as mean with S.E.M. (n =3 biological replicates). A Welch's t-test was used to test for the statistical difference between indicated conditions. **** p < 0.0001.

C. Cytokine concentration in the culture media of HT29 / TO-ZBP1WT cells treated with 0 or 100 nM CpA and 0 or 50 ng/mL Dox as indicated for 24 h. Data is plotted as mean with S.E.M. (n = 3 biological replicates). Unpaired t-tests were used to test for the statistical difference between indicated conditions. ** p = 0.0049; * p = 0.0394.

D-F. Western blot analysis of anti-FLAG (ZBP1) immunoprecipitation from HT29 or HT29 / TO-ZBP1WT or HT29 / RIPK1-KO clone aA3 / TO-ZBP1WT cells treated with 0 or 500 ng/mL Dox for 16 h. Asterisk indicates antibody heavy chain signal in IP samples. Blots are representative of at least (D) two and (E-F) three biological replicates.
Human ZBP1 induces cell death-independent inflammatory signaling via RIPK3 and RIPK1 (2022)
Figure 6

Figure 6 - ZBP1 mediates SARS-CoV-2-induced cytokine production

A. Western blot analysis of ZBP1, RIPK1, RIPK3, MLKL levels in Calu-3 cell lines with stable expression of shRNAs targeting ZBP1 or a mismatch sequence (shMM), untreated (NT) or treated with 10 ng/mL IFNβ for 48 h. Blots are representative of two biological replicates.

B, C. Relative mRNA levels (B) or cytokine levels in the culture media (C) of indicated genes in Calu-3 cells infected with mock or SARS-CoV-2 viruses at indicated MOIs for 16, 24, 48 or 72 hours. Data is plotted as mean with S.E.M. (n = 3 biological replicates). Two-way ANOVA and Tukey's (B) or Dunnet's (C) multiple comparison test were used to test for statistical differences between each infected sample and mock-treated sample and between the two different MOIs at 72 h time point. For (B): **** p < 0.0001; *** p = 0.0006, ** p = 0.0022 for ZBP1, p = 0.0072 for CXCL10; ns = not significant (p > 0.05). For (C): **** p < 0.0001; *** p = 0.0002; * p = 0.0244; ns = not significant (p > 0.05).

D, E. Relative mRNA levels (D) or secreted cytokine levels (E) of indicated genes in Calu-3 cells knocked down against mismatch sequence (shMM) and ZBP1 at three different sites (shZBP1-50, shZBP1-52 and shZBP1-53) infected with mock or SARS-CoV-2 virus at MOI = 2 for 72 hours. Data is presented as mean with S.E.M. (n = 3 biological replicates). One-way ANOVA and Sidak's multiple comparisons test were used to test for statistical differences between indicated conditions. ns = not significant, * p<0.05; ** p<0.01; *** p<0.001; **** p<0.0001. See source data for statistical details.

F. Schematic model of the proposed ZBP1-induced signaling pathways for inflammatory responses and cell death in human cells.

Expanded View Figure legends
Inhibiting parasite proliferation using a rationally designed anti-tubulin agent (2021)
Figure 1

Figure 1: Protozoan and human tubulin and microtubule structures.

(A) Coomassie stained SDS-PAGE showing purified T. thermophila tubulin. (B) A representative cryo-electron micrograph of paclitaxel-stabilized T. thermophila MTs. (C) Kymographs obtained by TIRF microscopy showing the dynamics of T. thermophila MTs at the indicated concentrations in µM. (D) Plot of T. thermophila MT plus-end growth rates as a function of tubulin concentration. Error bars represent the mean +/- 95% CI. For each concentration, data is obtained from at least 2 independent experiments (n=41). (E) Cryo-electron microscopy density map of a 14 protofilament, paclitaxel-stabilized T. thermophila MT with pseudo helical symmetry applied. Left: outside view. The α- and β-tubulin monomers are shown in surface representation and colored in dark and light gray, respectively. Red arrow shows the location of the seam. Right: tubulin dimer models fitted into a sliced, transparent and zoomed-in view. The paclitaxel structure in stick representation is highlighted in magenta. Lateral contacts between protofilaments are indicated in blue (H2-S3 in α2 and β2), red (H1-S2 in α2 and β2) and green (M loop in α1 and β1). (F) Cartoon representation of the crystal structures of T. thermophila tubulin-D1 (left) and recombinant H. sapiens tubulin-D1 (right) complexes. Bound nucleotides are displayed in stick representation, the
Structural insights into actin filament recognition by commonly used cellular actin markers (2020)
Figure 5

Figure 5: Mutation analysis of utrophin:F-actin binding interface.

A. Representative Coomassie stained SDS-PAGE gels of UTRN-ABD and UTRN-V87D co-sedimentation with F-actin. Pellet (top) and supernatant (bottom) fractions of individual co-sedimentation reactions of increasing utrophin concentrations, uncropped gel images of all the co-sedimentation reactions are presented in Supplement Figure 6.

B. Apparent Kd indicated was calculated from the titration data of co-sedimentation assays of utrophin wildtype (1.8µM) and mutants; H29A (2.8µM), I22D (38µM), V87D (>100µM) and N109A (55µM) as indicated. Data points for each concentration were averaged from 3 independent experiments, error bars represent S.D between independent experiments.

C. Confocal images of U20S cells transfected with GFP tagged UTRN-mini and mCherry UTRN-ABD, stained with SIR-Actin shows F-actin structures, mainly stress fibers. Scale bar = 5µm.

D. Co-localization analysis by intensity plot of GFP UTRN-mini, mCherry UTRN-ABD and SiR-Actin fluorescence using line scan of the region as indicated by the yellow line in C.
RBM14 prevents assembly of centriolar protein complexes and maintains mitotic spindle integrity. (2015)
Figure 1

Depletion of RBM14 induces ectopic formation of centriolar protein complexes

A–E Mitotic control U2OS cells or U2OS cells treated with RBM14 siRNA were stained with antibodies against centrin-2 (green) and C-Nap1 (magenta) (A), Centrobin (green) and C-Nap1 (magenta) (B), centrin-2 (green) and CPAP (magenta) (C), acetylated-tubulin (green) and CP110 (magenta) (D), and centrin-2 (green) and γ-tubulin (magenta) (E). DNA is shown in blue. Insets show approximately twofold magnified views of fluorescent foci around the centrosome. Scale bar, 5 μm. Histograms on the right represent frequency of mitotic cells with excess foci of the indicated proteins at spindle poles in each condition. Values are mean percentages ± standard error of mean (SEM) from three independent experiments (n = 30 for each condition). *P < 0.05, **P < 0.01, n.s., not significant (one-tailed t-test). Note that we counted the number of C-Nap1 foci after anaphase in mitosis when C-Nap1 signals recover from the reduction in prometaphase.
RBM14 prevents assembly of centriolar protein complexes and maintains mitotic spindle integrity. (2015)
Figure 2

RBM14 can suppress centriole amplification in cells arrested in S phase

A U2OS cells or U2OS cells expressing FLAG–RBM14 full length (FL, aa1–669), N-terminal fragment (RBM14[N], aa1–150) or C-terminal fragment (RBM14[C], aa151–669) and treated with control siRNA or siRNA against 3′ UTR targeting endogenous RBM14 were stained with antibodies against FLAG as well as centrin-2. Histograms represent frequency of mitotic cells with excess centrin foci at spindle poles in each condition. Values are mean percentages ± SEM from three independent samples (n = 30 for each condition). **P < 0.01, n.s., not significant (one-tailed t-test).

B Schematic of full-length, truncated mutants and NES-fused and PACT-fused RBM14 proteins used in this figure.

C, D Cytoplasmic RBM14 could suppress centriole amplification in HU-treated cells. (C) U2OS cells or U2OS cells expressing FLAG-RBM14 FL or [C] and treated with or without HU were stained with antibodies against centrin-2 (green) and FLAG (magenta). (D) U2OS cells or U2OS cells expressing FLAG-RBM14 FL, FLAG-RBM14-NES or GFP-RBM14-PACT and treated with or without HU were stained with antibodies against FLAG (magenta, left) or GFP (magenta, right) as well as centrin-2 (green). Insets show approximately twofold magnified views of fluorescent foci around the centrosome. Scale bar, 10 μm. Histograms represent frequency of cells in interphase with excess centrin foci in each condition. The percentages of U2OS cells with centrosomal localization of the RBM14 full-length protein or mutants are shown below the immunofluorescence images. We counted only cells that had adequate intensity of FLAG or GFP signals and did not find any significant difference in the total expression levels of the exogenous RBM14 proteins. Values are mean percentages ± SEM from three independent experiments (n = 30 for each condition). **P < 0.01 (one-tailed t-test). Please note that cytoplasmic expression levels of GFP-RBM14-PACT are less than those of FLAG-RBM14 FL (˜0.5-fold) or FLAG-RBM14-NES (˜0.7-fold).
RBM14 prevents assembly of centriolar protein complexes and maintains mitotic spindle integrity. (2015)
Figure 5

Ectopic centriolar protein complexes can be the sites of microtubule nucleation

A Schematic of microtubule regrowth assay during mitosis in RBM14-depleted U2OS cells.

B–E Control U2OS cells or U2OS cells treated with siRNA targeting RBM14 were cold-treated for 30 min, followed by 30–60 min incubation at 37°C and stained with antibodies against centrin (magenta in (B) and (D)) or γ-tubulin (magenta in (E)) as well as α-tubulin (green). DNA is shown in blue. Insets show approximately twofold magnified views of fluorescent foci around the centrosome. Scale bar, 5 μm. Histograms represent the percentages of mitotic cells showing the indicated phenotype at each time point. Values are mean percentages ± standard error of mean (SEM) from three independent experiments (n = 30 for each condition). *P < 0.05, **P < 0.01 (one-tailed t-test).
Shp2 signaling suppresses senescence in PyMT‐induced mammary gland cancer in mice (2015)
Figure 1

Shp2 ablation or inhibition inhibits self‐renewal and induces senescence in cultured PyMT tumor cells

Scheme of Shp2 ablation in cultures of PyMT;Shp2fl/fl tumor cells using retroviruses, which expressed CreERT2‐GFP or control GFP.

Western blot analysis of Shp2 in control and Shp2 ko cells.

Immunofluorescence analysis of Ki67 on control and Shp2 ko cells at day 7. Scale bar, 50 μm.

Quantification of the numbers of Ki67+ cells shown in (C). Error bars represent SEM (n = 3). **P 0.01.

Sphere formation by control and Shp2 ko cells at day 7. Scale bar, 200 μm.

Quantification of the numbers of spheres formed by control and Shp2 ko cells shown in (E). Error bars represent SEM (n = 3). **P 0.01.

Growth kinetics of spheres formed by control and Shp2 ko cells by counting sphere cells at day 4, 7, and 12. Error bars represent SEM (n = 3).

SA‐β‐gal staining on spheres formed by control and Shp2 ko cells at day 7. Scale bar, 100 μm.

Quantification of the numbers of senescent cells in the spheres shown in (H). Error bars represent SEM (n = 3). **P 0.01.

Western blot analysis of H3K9me3, p27, p53 pS18 (Ser18‐phosphorylated p53), total p53, Shp2, and α‐tubulin in control and Shp2 ko cells.

SA‐β‐gal staining on spheres formed by control cells and those treated by the Shp2 inhibitor GS493 at 15 μM at day 7. Scale bar, 100 μm.

Quantification of the numbers of senescent cells shown in (K). Error bars represent SEM (n = 3). **P 0.01.

Quantification of the numbers of spheres formed by control cells and those treated by the Shp2 inhibitor GS493 at 15 μM. Error bars represent SEM (n = 3). **P 0.01. Statistical significance was assessed by Student's unpaired t‐test.
Shp2 signaling suppresses senescence in PyMT‐induced mammary gland cancer in mice (2015)
Figure 2

Shp2 activates the expression of Skp2, Aurka, and Dll1/Hey1 genes to suppress senescence in PyMT tumor cells

Heatmaps for cell cycle, DNA replication, and p53 target genes defined by gene ontology terms in control, Shp2 ko, and Shp2‐inhibited PyMT spheres at day 7.

qRT-PCR analysis of mRNA levels of Skp2, Aurka, Dll1, and Hey1 in control, Shp2 ko, and Shp2‐inhibited cells. Error bars represent SEM (n = 3).

SA‐β‐gal staining on control, Shp2 ko, and Shp2 ko cells with overexpression of Skp2, Aurka, or N3IC cDNA. Scale bar, 100 μm.

Quantification of the numbers of senescent cells shown in (C). Error bars represent SEM (n = 3). **P 0.01; ***P 0.001.

Quantification of the numbers of spheres formed by cells shown in (C). Error bars represent SEM (n = 3). *P 0.05; **P 0.01; and ***P 0.001. Statistical significance was assessed by Student's unpaired t‐test.

Scheme showing an overview of Shp2‐dependent signaling systems and target genes, which are involved in senescence and cell cycle programs in PyMT tumor cells.
Shp2 signaling suppresses senescence in PyMT‐induced mammary gland cancer in mice (2015)
Figure 3

Shp2 target genes Skp2, Aurka, and Dll1/Hey1 mediate the suppression of p27‐ and p53‐dependent senescence in PyMT tumor cells

SA‐β‐gal staining on control, Shp2 ko, and Shp2 ko cells with shRNA knockdown of p27 or p53. Scale bar, 50 μm.

Quantification of the numbers of senescent cells shown in (A). Error bars represent SEM (n = 3). **P 0.01.

Quantification of the numbers of spheres formed by cells shown in (A). Error bars represent SEM (n = 3). **P 0.01.

Western blot analysis of p27, p53, and α‐tubulin in control, Shp2 ko, and Shp2 ko cells with overexpression of Skp2, Aurka, or N3IC cDNAs. The numbers below indicate the relative ratios of band intensities between p27 and α‐tubulin or between p53 and α‐tubulin.

Western blot analysis of p27, p53, and α‐tubulin in PyMT cells treated with control (DMSO) or inhibitors against Skp2 (MLN4924), Aurora A (VX‐680), or Notch (DAPT) at the indicated concentrations. The numbers below indicate the relative ratios of band intensities between p27 and α‐tubulin or between p53 and α‐tubulin.

Quantification of the numbers of senescent cells in PyMT cells treated with control, MLN4924, MLN4924 plus p27 knockdown or MLN4924 plus p53 knockdown. Error bars represent SEM (n = 3). **P 0.01; NS, not significant.

Quantification of the numbers of senescent cells in PyMT cells treated with control, VX‐680, VX‐680 plus p27 knockdown, or VX‐680 plus p53 knockdown. Error bars represent SEM (n = 3). *P 0.05; NS, not significant.

Quantification of the numbers of senescent cells in PyMT cells treated with control, DAPT, DAPT plus p27 knockdown, or DAPT plus p53 knockdown. Error bars represent SEM (n = 3). **P 0.01; NS, not significant. Statistical significance was assessed by Student's unpaired t‐test.

Source data are available online for this figure.