EMBO/sd-character-level-ner huggingface dataset:
Z-projection of HeLa cells expressing GFP-centrin1 immunostained for p34-Arc (sub-domain Arp2/3) following prometaphase arrest and forced mitotic exit for 5min. N=3 independent experiments. Scale bar = 10µm and for zoom 2µm.
(F) PAT4 mRNA levels from MEFs transfected with control or Rab12 siRNA as revealed by reverse‐transcription PCR analyses. Gapdh was used as an internal control.
Immunoblot analyses of , XRCC1 and XRCC1-SUMO in whole cell extracts of mESCs XRCC1 SUMOylation before and after exposure to H2O2 (5 mM, 15 min).
B) Representative images of metaphases from YFP:CENP-A (green) HeLa cells treated with Control (top) or H2A.Z.2 (bottom) siRNA. The white arrowheads indicate the mis-aligned chromosomes. Scale bar: 10 μm. C) Representative images of metaphase spreads from Control (top) or H2A.Z.2 (bottom) siRNA-transfected HeLa cells after FISH with a Chr17 centromeric probe (green). The arrowheads indicate the separated sister chromatids. Scale bar: 10 μm.
(d) Western blotting results show the changes in TCF20 protein expression level during brain development. (e) Statistical analysis of normalized band intensity in the western blot results. n= 4 samples for each group.
B: Senescence-associated β-galactosidase staining of glomerular endothelial cells (GEnC) at early (p9) or late (p17) passage.
(C) Fluorescence intensity based analysis of pFTAA-positive area covered in the cortex of APP23p40+/+ (n=8) and APP23p40-/- (n=10) mice (left) and representative images for each genotype (right), scale bar = 1 mm. Mean ± s.e.m., statistical analysis: two-tailed unpaired t-test, p=0.3406.
(A) Schematic of the 3 human isoforms of the heterochromatin protein 1 (HP1). The N-terminal chromodomain of HP1 (in yellow) recognizes H3K9 methylation in vitro, with a preference for higher methylation states (H3K9me1>H3K9me2>H3K9me3), while the chromoshadow domain at its C-terminus (in blue) is involved in homo-/hetero-dimerization as well as interaction with other proteins containing a PXVXL motif. Both domains are separated by a hinge region (in brown).
(I) PI analysis of CTRL and CMB cells treated with CX-5461 and everolimus in the presence and absence of metformin for 48 hours as indicated.
(E) Sucrose gradient fractions (top) and western blot analysis (bottom) of the (CGA-CCG) dicodon-stalled RNC samples. After the translation reaction, the RNCs were affinity-purified as indicated in (C). The eluate was loaded on a 10-50 % sucrose gradient and fractionated. Each collected fraction was analysed using anti-HA antibody to detect uS10-HA. Note that disomes are preferentially polyubiquitinated over monosomes.
Correlation of mRNA expression of TBL1 and PIK3CA in human patient tumor tissue (normalized to 18S rRNA and relative to a pooled organ donor sample); n = 17 patients; P-value determined by testing for slope of regression line ≠ 0.
DNA combing analysis of replication. Graphs indicate the distribution of BrdU track length (kb) at 60 and 120 min after α‐factor release in the presence of 40 mM HU, the replication speed (kb/min) determined with the two time points analyzed and the inter‐origin distance (kb) at 60 min after release. The median test was applied.
C. Volcano plot presentation of the differently expressed transcripts in GRN-/- hiMGL treated with Ab1 comparison to WT hiMGL. Genes with more than 20% significantly changed expression are marked in purple (upregulated) or blue (downregulated). Data information: Data represent mean ± SEM. For statistical analysis the unpaired, two-tailed student`s t-test was performed, Statistical significance was set at *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001, *****, p < 0.00001, and ns, not significant.
B NF-kB activation following IL-33 treatment of BM-derived eosinophils. Dusp5+/+ or Dusp5-/- BM-derived eosinophils were treated with IL-33 (25 ng/ml) for the indicated times and cytoplasmic fraction isolated and analyzed for p-p65 (top) and total p65 (bottom) (left panels). Quantitation of p-p65 normalized to total p65 level shown on left is graphically depicted on the right.
Morphological parameters quantification for 5 and 15 months old mice after LPS injection
D Lack of correlation between MIAA and VEGF-D plasma measures (Spearman's rs n.s., not significant).
A. Real-time PCR analysis of IL-6, TNF-α and IFN-β mRNA in RAW264.7 cells stably overexpressing flag-RKIP, flag-S109A and flag-S109D, followed by infection with VSV (MOI, 0.1).
(A-C) Ciliary length measured by fluorescence microscopic analysis at 1 year of age (1y). (A) Representative immunostaining of the ciliary marker Gt335 (green) in longitudinal cryosections of PRC ciliary regions in WT and USH1C retinas. Counterstaining by DAPI, scale bar 10µm. (B) Gt335 staining at higher magnification and principle of quantifying ciliary length by Gt335 staining. Scale bar 500nm. (C) Length of connecting cilia (CC) appear elongated in USH1C when applying a Fiji script to immunostained histological sections (2 pigs, 1y, 1 retina each, number of examined connecting cilia is indicated, error bars represent SD, two-tailed Student's t tests, ****p<0.0001).
A Genes corresponding to the indicated proteins were replaced by wild‐type (wt) or Cdk phospho‐site mutant (xA) sequences and then conditionally fused to Clb2m or Clb2mΔCdk. Cytokinetic defects were scored by FACS analysis of DNA content as in Fig C. The individual values from two independent clones (red dots) as well as their average (bars) are shown. Student's t‐test was applied to compare matched wt and xA strains. c, control cells.
(A) The N-lobe kinase linker region of PI4KB is strongly conserved back to D. rerio. The N-lobe linker region of PI4KB sequences of the organisms indicated were analysed using Clustal Omega/ ESpript 3. The consensus PKA motif (RRXS) that is conserved back to D. rerio is indicated on the sequence, as well as the RL494EA point mutation.
(B) mRNA expression of each candidate gene in 4T1PT and 4T1LN cells was determined by RT-qPCR. Gapdh was used as an internal control.
(A) Schematic representation of the IgH and c-Myc chromosomal loci before and after translocation. Arrows and black bar indicate the positions of the PCR primers used to amplify the rearranged region and the probe for Southern hybridization, respectively.
HeLa cells were immunostained with anti-DNA (green) and anti-LETM1 (red) (A), or anti-LETM1 (green) and anti-MRPS18 (red). (B). Data information: Scale bars are 12 µm in the main images and 3 µm in offset magnifications
In-gel fluorescence imaging of SecYCF488A reveals a cross-linking product of ~80 kDa assigned to the FtsQC40xSecYC283 adduct ("SecYxFtsQ"). Bands for covalently cross-linked SecY dimer ("SecYxSecY"), and adducts of SecY and ribosomal proteins ("SecYxRiboP") are indicated. The nascent chain-specific adduct "SecYxFtsQ" does not depend on the presence of PE lipids.
Western blots showing increased ERK1/2 activity (pERK1/2) and Cdc6 expression in differentiating C2C12 cells 48 h after Myoparr and Ddx17 KD. Tubulin expression served as an internal control.
Raising cytosolic Ca2+ with ionomycin (1 μM) rescues the Tpcn1-/- and Tpcn2-/- phagocytic defect, whilst UTP (100 μM) and ML-SA1 (50 μM) only weakly rescue (n = 84-192 cells).
(A) Time-lapse 3D-SIM of T6SS assembly, contraction and disassembly by visualizing TssB-sfGFP in A. baylyi. Yellow arrows indicate examples of contact-dependent T6SS assembly pairs.
(D) Map of coincidence of the low expression (lowest 10% of expression levels) of the 7 top DPMs with the low expression of CFTR in GTEx lung samples (lowest 10% of expression levels, when symptoms would be present in CF patients (Ramalho et al, 2002; Kerem et al, 1997); each small rectangle inside the big rectangle represents one individual; all presented samples are those with low CFTR expression. Dark blue rectangles indicate samples with low expression of the listed DPM).
(A) (I) MDC staining in neutrophils treated with LPS, LTA, peptidoglycan (PGN), loxorubin (LOX) and R848 (400×). (II) Percentage of PMN with acidified vacuoles as detected by MDC staining. LPS (50 ng/mL) (bar 2: 69.67±8.21%), LTA (bar 3: 75.17±9.80%), peptidoglycan (bar 4: 77±6.96%), loxorubin (bar 5: 66.67±5.61%), R848 (bar 6: 69.5±7.45%), poly I:C (bar 7: 16.33±3.14%) and flagellin (bar 8: 19.83±5.16%)−treated cells compared with control conditions (bar 1: 14.5±4.97%). Data are representative of six independent experiments and presented as mean±SD; Wilcoxon matched−pairs test, *p<0.05, n.s.=not significant.
(B) Co-immunoprecipitation (Co-IP) of endogenous ZEB1 and FOSL1 or JUN in MDA-MB-231 cells shows co-precipitation of ZEB1 with FOSL1 and JUN.
Reduced EC proliferation in the kidney (p17) of in TfebiEC-/- mice. (B) Representative images of vessels of the kidney in control and TfebiEC-/- mice stained with anti-CD31 and Ki-67 antibodies (scale bars: 50 µm). Bar graph indicates the percent of EC Ki-67+ nuclei versus total nuclei co-localized with CD31+ vessels (mice n=6, mean±SEM; **p<0.001 versus control mice by Student's t-test). Podocin staining is shown to glomerular localization.
Representative genes were selected for modules identified on Venn diagram in Fig 1E and their expression pattern across all samples shown as a heatmap. Red font, pDC ISG (module A); green font, pDC MSG (module D); mixed red and green font, pDC ISG and MSG (module E); black font, non-ISG, non-MSG (module B). The relative mRNA expression levels for each gene (lanes) across biological samples (rows) are represented by colors according to the scale shown above the heatmap. For the legend of the symbols depicting the classes of biological samples above each column please refer to the symbol key in Fig 1D.
C) Western blot analysis for the expression of LC3BI-II. The lysosomal protease inhibitors E64d and pepstatin A (Inh) blocked the autophagic flux and inhibited the degradation of LC3B-II.
Protein levels of E2F7 and E2F8 during cell cycle progression. HeLa cells were synchronized by a double thymidine block and released into fresh medium. Cells were harvested at the indicated time points and an asynchronous (AS) condition was used as control. Protein levels were measured by immunoblotting and cell cycle progression was determined by flow-cytometry (shown in Fig EV 1A). The asterisk indicates the E2F7-specific band.
(E) ChIP-qPCR for TRF2 is shown for cells treated as in panel A using primers across the subtelomeres of 18q (left) or 13q (right).
C Principal Component Analysis (PCA) based on bulk RNA-sequencing of C57#1 DLP and C57#3 DLP mouse prostate organoids cultured in normal conditions (ENRAD) (n = 3 biological replicates, C57#1 DLP; n = 3 biological replicates, C57#3 DLP), upon acute A83-01 depletion (-A83-01, 24 hours) (n = 3 biological replicates, C57#1 DLP only) or adaptation (-A83-01, long-term) (n = 3 biological replicates, C57#1 DLP; n = 3 biological replicates, C57#3 DLP).
Freezing tolerance assays of the egr2-3 mutant and EGR2:EGR2G2A-Myc transgenic plants in egr2-3 mutant. Two-week-old seedlings grown on MS medium containing 0.8% agar at 22°C were treated at −5°C for 0-1.5 h (NA) or −8°C for 0-1.5 h (CA). survival rate is shown in (I). Data shown in (I) are mean values ± SEM of three biological replicates, each of which has three technical replicates. Asterisks indicate significant differences compared with wild type for the same treatment (*P < 0.05, **P < 0.01, two-tailed t-test); n. s., not significant.
(C) LMP1-negative or -positive NPC cells were treated with BKA (1 μM) or CATR (5 μM) for 24 h, Mitochondrial OCR assessed with the XF24 extracellular flux analyzer (Seahorse) under sequential treatment with oligomycin, FCCP, and antimycin A. Data are presented as means ± S.E.M. (n = 6, biological replicates per group). (D) Oxidative phosphorylation-related metrics based on OCR datas. Data are presented as means ± S.E.M. (paired t-test, n = 6, biological replicates per group, * p < 0.05,** p < 0.01).
B. Rpp30 is a subunit of RNase P (red), a ribozyme involved in pre-tRNA processing by cleaving the 5' tail. The RNase Z (blue) cuts the 3' tail of the pre-tRNA, and CCA motif is added, forming mature tRNA ready to bind an amino acid (aa).
Quantification of distribution of GFP+ transfected cells 1dpe upon CTRL and Ece2 KD by IUE (n=3 CTRL and 4 Ece2 KD brains; *P=0.044 in One-way ANOVA and Tukey's Multiple Pairwise Comparison; data shown as mean±SEM).
B-E Tethering assays using the indicated R-Luc-MS2-A95-MALAT1 reporters and MS2-HA-tagged TNRC6A-SD, AGO2 and NOT1 in HEK293T cells. R-Luc activity and mRNA levels were normalized to those of the F-Luc transfection control and set to 100% in cells expressing MS2-HA. Panels B,D show mean values ± standard deviations from three independent experiments. Panels C and E show Northern blots of representative RNA samples.
C, Clockwise rotation of tethered fliM(R94S)∆N ∆cheZ cells and fliM(R94L)∆N ∆cheZ cells expressing FliMN-CheY (strains EW731 and EW733, respectively) in the absence or presence of acetate (10 mM, pH 7.0). FliMN-CheY concentration was estimated to be ~4 mM by extrapolation of the calibration curves for which a similar CheY expression system was used. No clockwise rotation was observed when benzoate substituted for acetate. Each data point is the mean of a separate experiment. Black line is the mean of all experiments.
(M) BAT from 4‐mo‐old Con and KO mice (n=4). Values are mean±s.e. *P0.05, **P0.01, ***P0.001.
(e,k) Dual point mutations were prepared on the basis of predicted CL contact residues (e), and analysed for participation in mitophagy elicited by Rot or 6-OHDA (k). Inset: expression of GFP-LC3 plasmids (uncropped blots in Supplementary Fig. S7). UT, untransfected. Mean ± s.d. of n = 3 independent experiments for f-h, and n = 4 independent experiments for i,j (see Supplementary Table S4 for statistics source data); *P0.05 versus respective vehicle. †P0.05 versus toxin-treated wild type (WT).
a, Increase in ubiquitinated proteins in Atg7flox/flox; nestin-Cre mouse brain over time. Homogenates of P9, P18 and P56 brains from Atg7flox/+; nestin-Cre and Atg7flox/flox; nestin-Cre mice were immunoblotted with an anti-ubiquitin antibody. An anti-actin antibody was used as a loading control. Data shown are representative of three separate experiments. We observed no sex difference in the accumulation of ubiquitin in Atg7flox/flox; nestin-Cre mice.
(J) Intracellular lactate was measured in miR-CTL, miR-195, siCTL, and siMICU1 expressing OVCAR4, CP20, and OVSAHO cells. n=3, biological repeats *P<0.05, Student's t-test.
Measurement of RelA protein levels in RELA KO single cell clones generated in RPE1-hTERT cells. Measurement of RelB protein levels in RELB KO single cell clones generated in RPE1-hTERT cells.
MITOL deletion promoted the interaction between IRE1α and BIM under ER stress. MITOL-depleted HEK293 cells (KO) were generated using CRISPR-Cas9 system. Cells were co-transfected with indicated vectors 24 hours prior to Tu treatment for 12 hours. Cells were immunoprecipitated with anti-FLAG antibody, followed by immunoblotting with indicated antibodies.
C, D Immunohistochemical staining shows levels of VE-cad (C) and pVE-Cad (731) (D) in the duodenum tissue from COVID-19 patients and healthy controls. Scale bars, 100 μm. For each group, n=7. n, biologically independent samples (human specimen). Data information: All data are shown as mean ± SD. for (C) and (D), P values are determined by Student's t-test
(A) Left panel: mitochondrial fission activates AMPK. HEK293 cells were transfected with a mock vector (control), Bnip3, DRP1, Fis1 or co‐transfected with DRP1 and Fis1. Cells were collected 24 h later and lysates were analysed by immunoblotting. Right panel: immunoblotting analysis shows AMPK phosphorylation in EDL and soleus muscles during muscle atrophy. P‐AMPK/AMPK ratio analysed by densitometric analysis is indicated below the panels. (B-E) Inhibition of AMPK blocks Bnip3‐ and DRP1/Fis1‐mediated atrophy.
A, B. The relative YTHDF1-RIP enrichment ratio of the indicated genes in C666 cells (A) and CNE2EBV cells with induced EBV reactivation (24 h post TPA/NaB treatment) (B). The EEF1A1 mRNA known to contain m6A sites and RPL30 mRNA containing no m6A modification were used as positive and negative controls, respectively. BALF1 and BCRF1 containing no m6A modification, identified in this study, were used as viral negative controls. The fold enrichment was determined by calculating the 2-ΔCt of the RIP sample relative to the input sample. The mean of the fold enrichment by IgG was normalized to 1.
(A) Schematic representation of yeast growth assay. The model proteins consisted of an UbL domain and S. cerevisiae imidazoleglycerol-phosphate dehydratase (His3), followed by stop codon (no tail) or a 51 amino acid tail derived from subunit 9 of the Fo component of the Neurospora crassa ATPase (Su9) at the C-terminus. In his3 mutant cells, the absence of His3 protein causes a growth defect when grown on selective media. Stable His3 proteins escape proteasome degradation and rescue the his3 mutant cells from the growth defect.
B, Quantitative real-time PCR showing reduced mRNA levels for Esr1, Esr2 and Pgr and upregulation of Shank3 and Psd-95 in cochleae of 4 week old Wbp2-deficient mice compared to littermate controls (n=3 for each genotype). Hprt is used as relative control. Error bars: ±SD. Two-tailed student t test: p=0.03 for Psd-95; p=0.007 for Shank3; p=0.03 for Esr2; p=0.0016 for Esr1; p=0.037 for Pgr.
Micrographs depicting immunoreactivity for MEIS2 (E, F) priming factors in the LRCs (BrdU+ only) 7 days after ChP-specific miR-204 inhibition and scrambled control White arrows point out the primed LRCs, the arrowheads label the MEIS2 Dot plots depicting the proportion of LRCs immunoreactive for the priming proteins MEIS2 after ChP specific miR-204 interference.
C) hSSU72 down-regulation results in multi-telomeric signals (MTS) that are dependent on DNA replication. Visualization of mitotic spreads of HT1080 hSSU72 shRNA cells treated with aphidicolin and colcemid. Telomere FISH was carried out using a PNA-telomere probe. MTS are represented by arrows. Quantification of MTS per metaphase: n=4; **p ≤0.01 ****p ≤0.0001 based on a two-tailed Student's t-test to control sample. Error bars represent standard error of the mean (SEM).
(f,g) Northern blot analyses of TbMCU RNAi of BSF (f) and PCF (g) trypanosomes grown in the absence (0) and presence (2-8; 2-10) of tetracycline (top). Tubulin is shown as a loading control (bottom). Markers are shown on the right. The transcript of TbMCU, including the 5′- and 3′-UTR was ~1.5 kb in length.
(C) Immunofluorescence images of DAPI and γH2AX staining in p53-WT or KO RPE1 cells either before or 48 hours after release from a 7-day treatment with palbociclib (1.25μM). Scale bar = 250 μM, zoom inserts = 3x magnification of highlighted regions.
(D-E) Expression of PR1 (D) and PR2 (E) in the indicated genotypes as determined by quantitative RT-PCR. Values were normalized to the expression levels of ACTIN1. The data are shown as mean ± SD (n=3) with one-way ANOVA analysis and Tukey test (P < 0.01). Different letters indicate significant differences. The experiments were repeated three times with similar results.
(C) Streptavidin Western blotting of total biotinylated proteins in APEX2:RAB or APEX2 only Flp-In/T-REx HeLa cells.
A Schematic representation of WT WNV and WNV-poly(A) genomes. WT 3'UTR is represented by the diagram of secondary structure. Three regions are labeled as SL, stem-loop region; DB, dumbbell region; and 3'SL, stem loop region, respectively.
(A) To examine the levels of the V-ATPase V1-V0 holoenzyme in WT and NDST3 KO RPE1 cells, cytosolic and membrane fractions were analyzed by immunoblotting using antibodies against the V-ATPase subunits V1A (ATP6V1A), V1C1 (ATP6V1C1), and V0D (ATP6V0D). LAMP1 and vinculin were used as loading controls for membrane proteins and cytosolic proteins, respectively. (B) Quantification of the levels of ATP6V0D relative to LAMP1 in the membrane fraction from (A) (n = 3 independent experiments, P = 0.7786). Data information: Error bars represent ± standard deviation.
(B) Coomassie blue stained SDS-PAGE of carbohydrate recognition domain CRD1 and CRD2 of galectin-9. Data are representative of n=3 independent experiments.
I, Schematic diagram of SnRK1α protein structure showing catalytic (CD) and regulatory (RD) domains. The CD includes the phosphorylated T-loop region. RD includes both kinase-associated 1 (KA1) and ubiquitin-associated (UBA) subdomains.
(B) Sequence alignment showing the introduction of wild-type or mutated RxL motif to Far1.
Effect of 24 h incubation with 250 ng/ml TRAIL on Nalm6 199R, Nalm6 199R BID KO #1 and Nalm6 199R BID KO #5, measured as DRAQ7+ cells and normalized to untreated Nalm6 199R cells. Each dot corresponds to the average normalized value of 3-5 technical replicates in n=3 independent experiments, *** p<0,001 with respect to untreated conditions.
A-C Immunoblot analysis stability of ARR1/10/12 and ARR1T553A/10S383A/12S323A proteins under salt stress. Seven-day-old seedlings of 35S:ARR1:MYC, 35S:ARR10:YFP, 35S:ARR12:YFP, 35S:ARR1T553A:MYC, 35S:ARR10S383A:YFP, and 35S:ARR12S323A:YFP were treated with or without 200 mM NaCl for indicated time points. Actin was used as the internal reference. The relative intensity of band detected by anti-MYC or anti-GFP antibody to that by anti-Actin antibody without treatment was set to 1.0. D-I Quantification analysis of stability of ARR1/10/12 and ARR1T553A/10S383A/12S323A proteins under salt stress in (A-C).
E Schematic diagram of the S1P domain structure. The p.Val355Gly variant is localized in the peptidase S8 domain, the c.2072-2A>T variant is located in the ABC transp-aux domain, and p.Ter1053Arg and p.Ter1053Cys are found in the cytoplasmic domain.
Representative images of tumors (E) and the tumor weight (F) of mice treated with oxaliplatin in the presence or absence of sEVs (n = 3 biological replicates; mean ± SEM; *P = 0.0488; two-tailed unpaired Student's t-test).
Computationally assembled CrSAS-6[6HR] single or double ring in register (ribbon diagram shown in different shades for clarity) fitted into the 3D maps of the 36 % T. mirabilis class (A, B) Dashed box shows longitudinal section through hub element (left), double chevron viewing point of longitudinal external views (right). Extra unaccounted densities in single ring fitting are indicated by arrowheads Note that each elongated hub density can accommodate two tightly stacked CrSAS-6[6HR] rings
E. Sensitivity to SHH signaling was significantly increased in primary fibroblasts from KV10.1 knockout mice, in agreement with the higher abundance of primary cilia. Cells were serum starved and SHH was stimulated after 24 hours by addition of culture supernatant of SHH-expressing HEK293 cells. Expression of mRNA for Gli1 was used as reporter of SHH activation by qRT-PCR.
A-B. Amino acid sequences of toxin S-subunits depicting (A) Mut1 (∆112-117) and (B) Mut2 (∆130-134) domains, based on ClustalW alignment.
H: Comparative flow cytometric analysis of Esrrb-2a-tdTomato and Nanog:GFP expression in undifferentiated SSEA-1+ TNG E-2a-tdT or Nanog-null ES∆N E-2a-tdT ESCs cultured for three days in GMEMβ/FCS/LIF. Data are shown as dot plots (top) and histogram (bottom).
f. K-mer statistics computation and resulting motif probability matrix depicting occurrences of amino acids in each position of all computed CDR3 beta chains.
B) Representative AP from WT-, LQT1R594Q- and JLNSR594Q-CMs, paced at 1 Hz, under baseline conditions (black), after application of 100 nM AST (red), and after addition of increasing concentrations of LUF7346 in the presence of AST (colour-code is shown).
Iron depletion rapidly reshapes the cellular metabolome. DFP treatment alters glucose utilization to promote lipid biosynthesis and TAG storage in lipid droplets via DGAT1 activity, upstream of NIX-dependent mitochondrial clearance. Without DGAT1, fatty acids cannot be esterified TAG, compounding lipid dysfunction that impairs lysosomal homeostasis, leading to inefficient mitophagy and promoting cell death. Strikingly, genetic depletion of DGAT1 in vivo also impairs basal mitophagy, demonstrating the physiological relevance of our in vitro findings.