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There are 113 results for Autophagy (displaying 1 to 10).

Inhibition of autophagy by TAB2 and TAB3

Autophagic responses are coupled to the activation of the inhibitor of NF‐κB kinase (IKK). Here, we report that the essential autophagy mediator Beclin 1 and TGFβ‐activated kinase 1 (TAK1)‐binding proteins 2 and 3 (TAB2 and TAB3), two upstream activators of the TAK1‐IKK signalling axis, constitutively interact with each other via their coiled‐coil domains (CCDs). Upon autophagy induction, TAB2 and TAB3 dissociate from Beclin 1 and bind TAK1. Moreover, overexpression of TAB2 and TAB3 suppresses …

Reduced interaction between Beclin 1, TAB and TAB3 in conditions of autophagy induction. (A, B) Inhibition of autophagy by dominant‐negative (DN) TAK1. HeLa cells were co‐transfected with a GFP–LC3‐encoding construct plus pcDNA3.1 (empty vector), or plasmids for the expression of WT TAK1 (TAK1WT) or the DN TAK1K63W mutant. One day later, cells were either left untreated (control) or driven into autophagy by starvation or by the administration of 1 μM rapamycin or 30 μM pifithrin α (PFTα …

Inhibition of autophagy by full‐length TAB2 and TAB3 but induction by their C‐terminal fragments. (A) Effects of full‐length TAB2 and TAB3 or their deletion mutants (as in Figure 1C) on autophagy. HeLa cells stably expressing GFP–LC3 were transfected with pcDNA3.1 (empty vector) or with plasmids encoding the indicated TAB2 and TAB3 variants for 24 h, then driven into autophagy by starvation or by the administration of 1 μM rapamycin or 30 μM pifithrin α (PFTα) for 4 h. Finally, the frequency …

Induction of autophagy by a Beclin 1 fragment that disrupts the interaction between endogenous Beclin 1, TAB2 and TAB3. (A) Determination of the TAB‐binding domain (TBD) within Beclin 1 (BCN1). Yeast two‐hybrid technology was used to screen for positive (+) or negative interactions (−) between BCN1 fragments and full‐length TAB2. (B) Schematic presentation of the constructs used in subsequent experiments (BBD, Beclin‐binding domain). (C) Confirmation of the TBD by immunoprecipitation …

… Macroautophagy (hereafter referred to as ‘autophagy’) is a catabolic pathway involving the sequestration of cytoplasmic material in double‐membraned vesicles, the autophagosomes. Upon fusion with lysosomes, autophagosomes become autophagolysosomes and their content gets degraded by acidic hydrolases, allowing nutrients and macromolecules to fuel cellular metabolism or sustain stress responses ( ; ). Multiple distinct perturbations of the cellular physiology can induce autophagy through …

Alfredo Criollo et al. The EMBO Journal December 2011

Modulation of intracellular ROS levels by TIGAR controls autophagy

The p53‐inducible TIGAR protein functions as a fructose‐2,6‐bisphosphatase, promoting the pentose phosphate pathway and helping to lower intracellular reactive oxygen species (ROS). ROS functions in the regulation of many cellular responses, including autophagy—a response to stress conditions such as nutrient starvation and metabolic stress. In this study, we show that TIGAR can modulate ROS in response to nutrient starvation or metabolic stress, and functions to inhibit autophagy. The ability …

TIGAR expression modulates autophagy in response to nutrient starvation or metabolic stress. (A) (Left panel) Confocal microscopic images of the fluorescence in U2OS cells stably over‐expressing Flag‐tagged‐TIGAR (clone TIGAR#7) or control cells (clone Cont#1) and infected with an adenovirus expressing GFP‐LC3 for 16 h. Cells were then left untreated, exposed to nutrient starvation for 6 h or to metabolic stress for 24 h. (Right panel) Quantitation of the percentage of GFP‐LC3–positive cells …

TIGAR expression modulates autophagy independently of p53. (A) Quantitation of the percentage of GFP‐LC3–positive cells displaying GFP puncta. U2OS cells stably expressing GFP‐LC3 were transfected with scrambled or TIGAR siRNAs, and 48 h after transfection, cells were left untreated (t0) or treated with Bafilomycin A1 (100 nM) for 1 or 2 h (t1 and t2). The percentage of cells with GFP‐LC3 puncta was calculated at the indicated time points. Data are shown as the mean and standard deviation from …

TIGAR modulation of autophagy influences apoptosis. (A) Quantitation of the percentage of GFP‐LC3 puncta positive cells. U2OS cells stably over‐expressing Flag‐tagged‐TIGAR (clones TIGAR#5 and TIGAR#7) or control cells (clones Cont#1 and Cont#3) were left untreated or exposed to nutrient starvation for 6 h, with or without treatment with Z‐VAD‐FMK for 24 h. The percentage of cells with GFP‐LC3 puncta was calculated, and data are shown as the mean and standard deviation of the mean from three …

Autophagy—a mechanism that results in lysosomal degradation of cytoplasmic constituents—is a critical response to metabolic stress ( ; ). Limited autophagy in response to nutrient starvation has been shown to provide a survival function, and specific removal of damaged mitochondria by autophagy can also help prevent the activation of apoptotic pathways ( ). However, in some systems, the induction of autophagy has been shown to contribute to, or enhance, the apoptotic response …

Karim Bensaad et al. The EMBO Journal October 2009

Loss of autophagy in hypothalamic POMC neurons impairs lipolysis

Autophagy degrades cytoplasmic contents to achieve cellular homeostasis. We show that selective loss of autophagy in hypothalamic proopiomelanocortin (POMC) neurons decreases α‐melanocyte‐stimulating hormone (MSH) levels, promoting adiposity, impairing lipolysis and altering glucose homeostasis. Ageing reduces hypothalamic autophagy and α‐MSH levels, and aged‐mice phenocopy, the adiposity and lipolytic defect observed in POMC neuron autophagy‐null mice. Intraperitoneal isoproterenol restores …

POMC neuron‐selective loss of autophagy. (A) Immunofluorescence for POMC (green) and Cre (red; n=4), (B) POMC (green) and Atg7 (red; n=4) and (C) POMC (green) and p62 (red; n=6) in MBH sections from Con and Atg7F/F‐POMC‐Cre (KO) mice. (D) TUNEL‐positivity (green; n=4) and (E) number of POMC‐positive neurons (red) in MBH sections from Con and KO mice (n=6). Values are mean±s.e.m. P values are as compared with diet‐ and age‐matched controls. *P<0.05, ***P<0.001. Nuclei are blue (DAPI). Scale …

POMC neuronal autophagy is required for lipolysis. (A) Percent loss of body fat and (B) lean mass in 24‐h‐fasted Con and KO mice on RD or HFD (n=6–8). (C) Histology for eWAT from fed or 6‐h‐fasted Con and KO mice on RD (n=3–4). (D) Serum fatty acids and (E) glycerol from fed or 6‐h‐fasted Con and KO mice on RD (n=7–9). (F) Serum fatty acids and (G) glycerol after intraperitoneal isoproterenol (Iso) in 6‐h‐fasted Con and KO mice on RD (n=5–6). (H) Immunoblot for oxidized proteins in eWAT from RD …

Ageing reduces POMC neuronal autophagy and lipolysis. (A) Immunoblots for Atg7 in MBH from young (3 mo), middle‐aged (12 mo) and aged (22 mo) fed and 6‐h‐fasted (Stv) mice (n=4), and (B) LC3‐II in MBH explants from 3 mo and 22 mo fed mice in presence or absence of lysosomal inhibitors (Inh) (n=11–13). Mean±s.e.m values for (B) steady‐state LC3‐II and (C) LC3‐II flux are shown (n=11–13). (D) Immunoblots for p62 and NBR1 flux in MBH from 3 mo and 22 mo fed mice in presence or absence of Inh (n=11 …

… (MSH) [ ]. α‐MSH activates central melanocortin receptors to curtail food intake and promote energy expenditure by modulating sympathetic outputs to the periphery [ ]. Macroautophagy (hereafter autophagy) maintains cellular homeostasis by sequestering cytosolic cargo within autophagosomes and delivering these to lysosomes for degradation [ ]. The ubiquitin E1‐like ligase, Atg7 initiates membrane elongation by mediating LC3 (microtubule‐associated light chain 3) and Atg5‐12 conjugation …

Susmita Kaushik et al. EMBO Reports March 2012

Mitochondria regulate autophagy by conserved signalling pathways

Autophagy is a conserved degradative process that is crucial for cellular homeostasis and cellular quality control via the selective removal of subcellular structures such as mitochondria. We demonstrate that a regulatory link exists between mitochondrial function and autophagy in Saccharomyces cerevisiae . During amino‐acid starvation, the autophagic response consists of two independent regulatory arms—autophagy gene induction and autophagic flux—and our analysis indicates that mitochondrial …

Model for the role of mitochondrial function in autophagy regulation under amino‐acid starvation. Amino‐acid starvation induces the two regulatory arms of the autophagic response, ATG8 induction and autophagic flux. Autophagic flux is regulated in an Atg1, PKA, and TORC1‐dependent manner, while ATG8 induction is regulated by PKA. Mitochondrial respiratory deficiency induces PKA activity and, thereby, suppresses both arms of the autophagic response.

Role of TORC1 in autophagy regulation under amino‐acid starvation. (A) Wild‐type, rho0, Δnpr2, and Δnpr2 rho0 cells expressing prATG8‐GFP‐ATG8 (upper panel) or prATG8‐GFP (lower panel) were exposed to amino‐acid starvation medium supplemented with galactose in the absence or presence of rapamycin. Samples were analysed as described in Figure 1A. The means and s.d. of four (n=4) independent experiments are indicated. (B) Wild‐type, rho0, Δnpr2, and Δatg7 cells expressing prNPR1‐NPR1‐HA were …

Mitochondrial function controls autophagy by modulating PKA activity. (A) PKA‐dependent regulation of the autophagic response under amino‐acid starvation. Wild‐type, rho0, pka, and ras2G19V‐expressing cells harbouring prATG8‐GFP‐ATG8 (upper panels) or prATG8‐GFP (lower panels) were exposed to amino‐acid starvation medium supplemented with galactose. PKA activity in pka was inhibited by addition of 1NM‐PP1 (PP1; 1 μg/ml). Samples were analysed as described in Figure 1A; autophagic flux …

Autophagy is a highly conserved and regulated process essential for the degradation of long‐lived proteins and organelles in eukaryotic cells. During autophagy, cytosolic content is sequestered via de novo formation of double‐membrane‐bounded structures termed autophagosomes. The autophagosomal outer membrane docks and fuses with the vacuole and the inner membrane vesicle is subsequently released and degraded by resident hydrolases to generate metabolic building blocks for biosynthesis …

Martin Graef et al. The EMBO Journal June 2011

Control of autophagy initiation by phosphoinositide 3‐phosphatase jumpy

The majority of studies on autophagy, a cytoplasmic homeostatis pathway of broad biological and medical significance, have been hitherto focused on the phosphatidylinositol 3‐kinases as the regulators of autophagy. Here, we addressed the reverse process driven by phosphoinositide phosphatases and uncovered a key negative regulatory role in autophagy of a phosphatidylinositol 3‐phosphate (PI3P) phosphatase Jumpy (MTMR14). Jumpy associated with autophagic isolation membranes and early …

Jumpy R336Q mutant associated with centronuclear myopathy is defective in inhibiting autophagy. (A–K) C2C12 cells were transfected for 48 h with YFP, YFP‐Jumpy WT (Jumpy WT), YFP‐Jumpy C330S (Jumpy CS), YFP‐Jumpy Y462C (Jumpy YC) or YFP‐Jumpy R336Q (Jumpy RQ), fixed and immunostained with anti‐p62 antibody (red). p62 puncta were quantitated by confocal fluorescence microscopy. Representative confocal images of YFP (A), YFP‐Jumpy WT (B), YFP‐Jumpy C330S (C), YFP‐Jumpy Y462C (D) and YFP‐Jumpy …

Screening of active members of the myotubularin family identifies Jumpy as a negative regulator of autophagy. (A) Domains and members of catalytically active myotubularins. Asterisks, Jumpy mutations found in patients with centronuclear myopathy. C330S, R336Q and Y462C, Jumpy mutants used in this study. (B) RAW 264.7 cells transfected for 48 h with control (sc), MTMR6 or Jumpy siRNA, were pretreated for 30 min with 100 nM Bafilomycin A1 (BafA1), 10 μg/ml E64d and 10 μg/ml pepstatin …

Autophagy is an ancient, highly conserved eukaryotic intracellular homeostatic process carrying out degradation of cytoplasmic components including damaged or superfluous organelles, toxic protein aggregates and intracellular pathogens ( ; ; ). Autophagy takes place at basal levels in all eukaryotic cells, turning over long‐lived macromolecules and large supra‐molecular structures including whole organelles. In addition to its housekeeping role, autophagy can be upregulated during metabolic …

Isabelle Vergne et al. The EMBO Journal August 2009

XIAP inhibits autophagy via XIAP‐Mdm2‐p53 signalling

The primary role of autophagy is adaption to starvation. However, increasing evidence suggests that autophagy inhibition also plays an important role in tumorigenesis. Upregulation of X‐linked inhibitor of apoptosis (XIAP) has been associated to a variety of human cancers, yet the underlying mechanisms remain obscure. Here, we report that XIAP suppresses autophagy by exerting a previously unidentified ubiquitin E3 ligase activity towards Mdm2, which is a negative regulator of p53. XIAP controls …

XIAP‐modulated autophagy is associated with the tumorigenecity. (A–C) 1 × 106 HCT116 XIAP WT and 1 × 106 XIAP KO cells (group 1), 1 × 106 HCT116 XIAP KO cells (KO‐Ctrl) and 1 × 106 HCT116 XIAP KO cells stably expressing wild‐type XIAP (KO‐XIAP) (group 2), 1 × 106 HCT116 XIAP KO cells (KO‐Ctrl) and 1 × 106 HCT116 XIAP KO cells stably expressing XIAP S87A mutant (KO‐XIAP SA) (group 3), or 1 × 106 HCT116 XIAP KO cells (KO‐Ctrl) and 1 × 106 HCT116 XIAP KO cells stably expressing XIAP S87D mutant …

XIAP inhibits autophagy via the Mdm2‐p53 pathway. (A) A549 and IMR90 cells were transfected with XIAP‐specific or control siRNAs. Cell lysates were subjected to western blot analysis with the indicated antibodies. The data are representative of two biological replicates. The ratio of LCII/LC3I to actin is presented in Supplementary Figure S2A. (B) HCT116 cells expressing XIAP‐specific or control siRNAs, HCT116 XIAP WT and XIAP KO cells were individually transfected with Flag‐XIAP or control …

XIAP regulates serum starvation‐induced autophagy. (A) HCT116 XIAP WT and XIAP KO cells were treated with EBSS for the indicated periods of time. GFP‐LC3 puncta formation was observed by a microscope. Quantification of LC3 punctate cells was shown on the right. The data are represented as means±s.d. of three independent experiments. (B) HCT116 XIAP WT and XIAP KO cells were treated with EBSS for 4 h followed by western blot analysis with the indicated antibodies. The data are representative …

Autophagy is an intracellular bulk degradation process that mediates the clearance of most long‐lived proteins and damaged organelles ( ; ). Upon induction of autophagy, cytosolic proteins and organelles are first sequestered within multimembrane‐bound autophagosomes and subsequently delivered to lysosomes, where the autophagic cargo undergoes protease‐dependent degradation ( ). The basal level of autophagy is important for maintaining normal cellular homeostasis. Inhibition of basal autophagy

Xing Huang et al. The EMBO Journal August 2013

HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy

Autophagy is primarily considered a non‐selective degradation process induced by starvation. Nutrient‐independent basal autophagy, in contrast, imposes intracellular QC by selective disposal of aberrant protein aggregates and damaged organelles, a process critical for suppressing neurodegenerative diseases. The molecular mechanism that distinguishes these two fundamental autophagic responses, however, remains mysterious. Here, we identify the ubiquitin‐binding deacetylase, histone deacetylase‐6 …

HDAC6 is not required for starvation‐induced autophagy. (A) Autophagosome–lysosome fusion is analysed in wild‐type and HDAC6 KO MEFs with or without starvation (6 h) using mCherry‐GFP‐LC3 as described in Figure 2A. (B) Wild‐type and HDAC6 KO MEFs were cultured in Hank's solution for 3 h followed by immunoblotting with an antibody for LC3, HDAC6, and GAPDH. (C) Long‐lived protein degradation in wild‐type and HDAC6 KO MEF cells. The degradation of [14C]‐valine labelled long‐lived protein was measured in the presence or absence of 3‐methyl adenine (3MA, inhibits the formation of autophagic vacuoles). The average of percentage degradation from three independent experiments is presented. The error bar represents the standard deviation.

Cortactin is recruited to protein aggregates and required for efficient autophagosome–lysosome fusion in homeostatic autophagy. (A) Wild‐type and HDAC6 KO MEFs were treated with MG132 and immunostained with antibodies against cortactin (red), ubiquitin (green), and phalloidin for F‐actin (blue) as indicated. The arrows indicated ubiquitin‐positive aggregates that were colocalized with F‐actin and cortactin. (B) Wild‐type MEFs were transfected with control or cortactin siRNA, treated with MG132 …

… Macro‐autophagy—hereafter referred to as autophagy—is the primary degradation pathway responsible for the disposal of long‐lived proteins, macromolecular complexes, and organelles ( ). Autophagy consists of two discrete but essential steps: formation of autophagosomes that sequester cytosolic constituents, and delivery of autophagic substrates to lysosomes where the contents are degraded (reviewed by ). The extraordinary ability of autophagosomes to sequester substrates of diverse sizes …

Joo‐Yong Lee et al. The EMBO Journal June 2010

WASH inhibits autophagy through suppression of Beclin 1 ubiquitination

Autophagy degrades cytoplasmic proteins and organelles to recycle cellular components that are required for cell survival and tissue homeostasis. However, it is not clear how autophagy is regulated in mammalian cells. WASH (Wiskott–Aldrich syndrome protein (WASP) and SCAR homologue) plays an essential role in endosomal sorting through facilitating tubule fission via Arp2/3 activation. Here, we demonstrate a novel function of WASH in modulation of autophagy. We show that WASH deficiency causes …

Lysine 437 ubiquitination of Beclin 1 is required for autophagy induction. (A) Endogenous Beclin 1 is ubiquitinated through K63 linkage during the process of autophagy. HeLa cells starved in EBSS for the indicated times were lysed and immunoprecipitated with anti‐Beclin 1 antibody. Immunoprecipitates were dissociated with 1% SDS and re‐immunoprecipitated with anti‐Beclin 1 antibody, followed by immunoblotting with antibody specific for lysine 63‐linked poly‐ubiquitin chains (anti‐K63‐Ub). (B …

WASH is localized in autophagosomes. (A) WASH colocalizes with GFP‐LC3 upon starvation. HeLa cells stably expressing GFP‐LC3 were stained with anti‐WASH antibody after treatment with EBSS or culture medium (CM) for 1 h. (B) Autophagy‐related WASH does not colocalize with EEA1. HeLa cells stably expressing GFP‐LC3 were cultured with EBSS for 1 h and stained with antibodies against EEA1 and WASH. (C) WASH localizes to unclosed autophagosomes. HeLa cells stably expressing GFP‐Atg5 were transfected …

WASH deficiency causes embryonic lethality and extensive autophagy. (A) Strategy to generate WASH‐knockout (WASH−/−) mice. The coding exons of mWASH gene were shown as white boxes. The target vector with exon3 of mWASH gene was flanked with two loxP sites (arrow) and one neomycin resistance gene. The primers used for genotyping were KO primers for deficient genotypes, loxP primers for loxP site identification, and Southern blot probe for floxed mWASH gene. KO, knockout, m, mouse. (B) Detection …

… Macroautophagy (herein referred to as autophagy) degrades cytoplasmic proteins and organelles to recycle cellular components that are required for cell survival and tissue homeostasis ( ; ; ; ). During autophagy induction, double‐membrane vesicles called autophagosomes are produced to sequester intracellular cargos and fused with lysosomes to form autolysosomes for subsequent degradation. Many autophagy‐related genes (Atg) have been identified and characterized in yeast and some of them …

Pengyan Xia et al. The EMBO Journal October 2013

Coordinated regulation of autophagy by p38α MAPK through mAtg9 and p38IP

Autophagy, a lysosomal degradation pathway, is essential for homeostasis, development, neurological diseases, and cancer. Regulation of autophagy in human disease is not well understood. Atg9 is a transmembrane protein required for autophagy, and it has been proposed that trafficking of Atg9 may regulate autophagy. Mammalian Atg9 traffics between the TGN and endosomes in basal conditions, and newly formed autophagosomes in response to signals inducing autophagy. We identified p38IP as a new …

Model for regulation of autophagy through mAtg9, p38IP, and p38 MAPK. In full medium, mAtg9 traffics between the TGN and endosomes. Autophagy is inhibited by phosphorylated p38α. p38IP is found in the pool of mAtg9 in peripheral endosomes, and in complex with p38α. It should be noted that the two pools of p38α–p38IP are identical and shown separately for clarity. In starvation, p38α is dephosphorylated and binds p38IP with a lower affinity, and can no longer inhibit autophagy (shown as a dashed line). The pool of p38IP released from p38α would facilitate mAtg9 trafficking and autophagy.

Activation of p38 inhibits autophagy and mAtg9 trafficking. (A) 293/GFP–LC3 cells were treated with 10 μM anisomycin for 30 min, or exposed to UV irradiation for 3 min followed by a 40‐min recovery and incubation in full medium, full medium with leupeptin, EBSS, or EBSS with leupeptin for 2 h. Cells were then fixed and visualized by confocal microscopy. GFP–LC3‐positive structures per cell were quantified as in Figure 3A. Bars=5 μm. Data are represented as mean±s.e.m. n=60 cells, mock versus …

p38IP is required for mammalian autophagy.(A) 293/GFP–LC3 cells were transfected with control or p38IP siRNA. At 72 h after transfection, cells were incubated in either full medium (FM), full medium with leupeptin (FM Leu), EBSS (ES), or EBSS with leupeptin (ES Leu) for 2 h. FM Leu (data not shown) is identical to FM alone. Quantification of GFP–LC3‐positive autophagosome number was performed by counting in a blinded experiment. Bars=5 μm (data are represented as mean±s.e.m. of 60 cells, ***P …

Autophagy is a highly regulated mechanism allowing survival during times of cellular stress or nutrient deprivation. On initiation of autophagy, an elongating membrane, termed the isolation membrane or phagophore in mammalian cells, enwraps a portion of cytoplasm. Fusion of the edges of the membrane forms a double‐membrane vesicle called an autophagosome. The autophagosome then fuses with endosomes and lysosomes forming an autolysosome in which the sequestered content is degraded (for review …

Jemma L Webber et al. The EMBO Journal January 2010

Species‐specific impact of the autophagy machinery on Chikungunya virus infection

Chikungunya virus (CHIKV) is a recently re‐emerged arbovirus that triggers autophagy. Here, we show that CHIKV interacts with components of the autophagy machinery during its replication cycle, inducing a cytoprotective effect. The autophagy receptor p62 protects cells from death by binding ubiquitinated capsid and targeting it to autophagolysosomes. By contrast, the human autophagy receptor NDP52—but not its mouse orthologue—interacts with the non‐structural protein nsP2, thereby promoting viral replication. These results highlight the distinct roles of p62 and NDP52 in viral infection, and identify NDP52 as a cellular factor that accounts for CHIKV species specificity.

Autophagy components promote CHIKV infection and control virus‐induced cell death in HeLa cells. Cells were mock infected or infected and immunoblotted for actin, p62 (A) or LC3 (B). Cells were infected for 15 h and labeled using antibodies to p62 and capsid (C). Cells were transfected with GFP‐LC3‐B, infected for 15 h and labeled with anti‐capsid antibody (D). Mice were infected for 3 days, then whole‐cell lysates of muscle were immunoblotted for LC3 or actin (E) and muscle sections were …

Autophagy receptors p62 and NDP52 localize to distinct pools of capsid and have distinct effects on CHIKV infection in Hela cells. Cells were infected for 15 h and labeled using antibodies to NDP52 and capsid (A), to p62, NDP52 and capsid (B), to NDP52, LC3‐C or capsid (C), to p62, ubiquitin (FK2) and capsid (D), or to NDP52, ubiquitin (FK2), and capsid (E). Cells were treated with CTRL or p62 siRNA, then infected for 24 h. Cell mortality (that is, fold change relative to mock‐infected cells …

… component of RCs, serves as a trigger for cell shutoff and induction of apoptosis in SINV‐ and CHIKV‐infected cells [ , ]. These functions are related to nsP2 nuclear location and assigned to its carboxy‐terminal domain [ ]. Autophagy is a cellular catabolic process, which sequesters cytosolic components within double‐membrane vesicles and targets them for degradation in lysosomes [ ]. While autophagy was initially thought to be non‐selective, evidence suggests a selective autophagic degradation …

Delphine Judith et al. EMBO Reports June 2013
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