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Autophagosome biogenesis: From membrane growth to closure

https://doi.org/10.1083/jcb.202002085

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/1873-3468.12901openalex-snapshot

Differential requirement for ATG2A domains for localization to autophagic membranes and lipid droplets

inferredcites →https://doi.org/10.1002/embr.201337995openalex-snapshot

TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation of autophagy

inferredcites →https://doi.org/10.1002/jcb.23399openalex-snapshot

AMPK promotes skeletal muscle autophagy through activation of forkhead FoxO3a and interaction with Ulk1

inferredcites →https://doi.org/10.1007/978-1-4939-8873-0_10openalex-snapshot

Formation of Autophagosomes Coincides with Relaxation of Membrane Curvature

inferredcites →https://doi.org/10.1007/s00018-015-2034-8openalex-snapshot

Autophagy signal transduction by ATG proteins: from hierarchies to networks

inferredcites →https://doi.org/10.1007/s00232-005-7006-8openalex-snapshot

Structure of Fully Hydrated Fluid Phase Lipid Bilayers with Monounsaturated Chains

inferredcites →https://doi.org/10.1016/0014-5793(93)80398-eopenalex-snapshot

Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1016/0014-5793(94)00672-5openalex-snapshot

Isolation of autophagocytosis mutants of Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1016/j.arr.2009.06.001openalex-snapshot

Age-related changes in total and regional fat distribution

inferredcites →https://doi.org/10.1016/j.bbalip.2019.03.005openalex-snapshot

ER platforms mediating autophagosome generation

inferredcites →https://doi.org/10.1016/j.ccell.2017.11.005openalex-snapshot

MST4 Phosphorylation of ATG4B Regulates Autophagic Activity, Tumorigenicity, and Radioresistance in Glioblastoma

inferredcites →https://doi.org/10.1016/j.cell.2007.05.021openalex-snapshot

Atg8, a Ubiquitin-like Protein Required for Autophagosome Formation, Mediates Membrane Tethering and Hemifusion

inferredcites →https://doi.org/10.1016/j.cell.2010.04.009openalex-snapshot

Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation

inferredcites →https://doi.org/10.1016/j.cell.2011.06.022openalex-snapshot

SNARE Proteins Are Required for Macroautophagy

inferredcites →https://doi.org/10.1016/j.cell.2012.11.001openalex-snapshot

The Hairpin-type Tail-Anchored SNARE Syntaxin 17 Targets to Autophagosomes for Fusion with Endosomes/Lysosomes

inferredcites →https://doi.org/10.1016/j.cell.2012.12.016openalex-snapshot

Differential Regulation of Distinct Vps34 Complexes by AMPK in Nutrient Stress and Autophagy

inferredcites →https://doi.org/10.1016/j.cell.2013.08.044openalex-snapshot

Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes

inferredcites →https://doi.org/10.1016/j.cell.2018.09.048openalex-snapshot

Biological Functions of Autophagy Genes: A Disease Perspective

inferredcites →https://doi.org/10.1016/j.cell.2019.12.005openalex-snapshot

Local Fatty Acid Channeling into Phospholipid Synthesis Drives Phagophore Expansion during Autophagy

inferredcites →https://doi.org/10.1016/j.celrep.2015.10.011openalex-snapshot

RACK1 Promotes Autophagy by Enhancing the Atg14L-Beclin 1-Vps34-Vps15 Complex Formation upon Phosphorylation by AMPK

inferredcites →https://doi.org/10.1016/j.celrep.2019.07.036openalex-snapshot

TOM40 Targets Atg2 to Mitochondria-Associated ER Membranes for Phagophore Expansion

inferredcites →https://doi.org/10.1016/j.cub.2007.07.029openalex-snapshot

ESCRT-III Dysfunction Causes Autophagosome Accumulation and Neurodegeneration

inferredcites →https://doi.org/10.1016/j.cub.2007.09.032openalex-snapshot

ESCRTs and Fab1 Regulate Distinct Steps of Autophagy

inferredcites →https://doi.org/10.1016/j.cub.2012.06.029openalex-snapshot

Phosphatidylinositol-3-Phosphate Clearance Plays a Key Role in Autophagosome Completion

inferredcites →https://doi.org/10.1016/j.cub.2018.03.002openalex-snapshot

The ER Contact Proteins VAPA/B Interact with Multiple Autophagy Proteins to Modulate Autophagosome Biogenesis

inferredcites →https://doi.org/10.1016/j.devcel.2011.02.006openalex-snapshot

LC3 and GATE-16 N Termini Mediate Membrane Fusion Processes Required for Autophagosome Biogenesis

inferredcites →https://doi.org/10.1016/j.devcel.2014.11.013openalex-snapshot

AMBRA1 Interplay with Cullin E3 Ubiquitin Ligases Regulates Autophagy Dynamics

inferredcites →https://doi.org/10.1016/j.devcel.2018.03.008openalex-snapshot

The RAB11A-Positive Compartment Is a Primary Platform for Autophagosome Assembly Mediated by WIPI2 Recognition of PI3P-RAB11A

inferredcites →https://doi.org/10.1016/j.devcel.2019.01.027openalex-snapshot

Phosphorylation of Syntaxin 17 by TBK1 Controls Autophagy Initiation

inferredcites →https://doi.org/10.1016/j.devcel.2019.02.013openalex-snapshot

Maturation and Clearance of Autophagosomes in Neurons Depends on a Specific Cysteine Protease Isoform, ATG-4.2

inferredcites →https://doi.org/10.1016/j.devcel.2019.06.016openalex-snapshot

Selective Autophagy of Mitochondria on a Ubiquitin-Endoplasmic-Reticulum Platform

inferredcites →https://doi.org/10.1016/j.febslet.2014.06.015openalex-snapshot

Regulation of autophagy: Modulation of the size and number of autophagosomes

inferredcites →https://doi.org/10.1016/j.jmb.2017.01.006openalex-snapshot

Sensing Membrane Curvature in Macroautophagy

inferredcites →https://doi.org/10.1016/j.jmb.2019.06.013openalex-snapshot

Physiological Stress Response by Selective Autophagy

inferredcites →https://doi.org/10.1016/j.jmb.2019.06.026openalex-snapshot

Phase Separation in Regulation of Aggrephagy

inferredcites →https://doi.org/10.1016/j.jmb.2019.06.032openalex-snapshot

Outstanding Questions in Mitophagy: What We Do and Do Not Know

inferredcites →https://doi.org/10.1016/j.jmb.2019.07.016openalex-snapshot

Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors

inferredcites →https://doi.org/10.1016/j.jmb.2019.10.027openalex-snapshot

Autophagosome Biogenesis Machinery

inferredcites →https://doi.org/10.1016/j.molcel.2008.03.003openalex-snapshot

AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint

inferredcites →https://doi.org/10.1016/j.molcel.2013.12.011openalex-snapshot

Early Steps in Autophagy Depend on Direct Phosphorylation of Atg9 by the Atg1 Kinase

inferredcites →https://doi.org/10.1016/j.molcel.2014.05.021openalex-snapshot

WIPI2 Links LC3 Conjugation with PI3P, Autophagosome Formation, and Pathogen Clearance by Recruiting Atg12–5-16L1

inferredcites →https://doi.org/10.1016/j.molcel.2014.12.007openalex-snapshot

PI(5)P Regulates Autophagosome Biogenesis

inferredcites →https://doi.org/10.1016/j.molcel.2015.05.031openalex-snapshot

Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates

inferredcites →https://doi.org/10.1016/j.molcel.2015.11.001openalex-snapshot

Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination

inferredcites →https://doi.org/10.1016/j.molcel.2017.08.005openalex-snapshot

The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity to Control ER-Isolation Membrane Contacts for Autophagosome Formation

inferredcites →https://doi.org/10.1016/j.molcel.2019.01.035openalex-snapshot

FIP200 Claw Domain Binding to p62 Promotes Autophagosome Formation at Ubiquitin Condensates

inferredcites →https://doi.org/10.1016/j.molcel.2019.01.041openalex-snapshot

The Cargo Receptor NDP52 Initiates Selective Autophagy by Recruiting the ULK Complex to Cytosol-Invading Bacteria

inferredcites →https://doi.org/10.1016/j.molcel.2019.02.010openalex-snapshot

Spatiotemporal Control of ULK1 Activation by NDP52 and TBK1 during Selective Autophagy

inferredcites →https://doi.org/10.1016/j.semcdb.2010.03.009openalex-snapshot

Regulation of macroautophagy in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1016/j.tcb.2015.08.010openalex-snapshot

Ubiquitin-Dependent And Independent Signals In Selective Autophagy

inferredcites →https://doi.org/10.1016/j.tcb.2019.01.008openalex-snapshot

Phase Separation, Transition, and Autophagic Degradation of Proteins in Development and Pathogenesis

inferredcites →https://doi.org/10.1016/s0378-1119(01)00614-xopenalex-snapshot

A genomic screen identifies AUT8 as a novel gene essential for autophagy in the yeast Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1038/cr.2012.24openalex-snapshot

Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein

inferredcites →https://doi.org/10.1038/cr.2013.169openalex-snapshot

Historical landmarks of autophagy research

inferredcites →https://doi.org/10.1038/cr.2014.84openalex-snapshot

Dapper1 promotes autophagy by enhancing the Beclin1-Vps34-Atg14L complex formation

inferredcites →https://doi.org/10.1038/cr.2014.85openalex-snapshot

RNF2 is recruited by WASH to ubiquitinate AMBRA1 leading to downregulation of autophagy

inferredcites →https://doi.org/10.1038/cr.2016.146openalex-snapshot

Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy

inferredcites →https://doi.org/10.1038/emboj.2009.159openalex-snapshot

Control of autophagy initiation by phosphoinositide 3‐phosphatase jumpy

inferredcites →https://doi.org/10.1038/emboj.2010.74openalex-snapshot

LC3 and GATE‐16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis

inferredcites →https://doi.org/10.1038/emboj.2012.225openalex-snapshot

Binding of the Atg1/ULK1 kinase to the ubiquitin‐like protein Atg8 regulates autophagy

inferredcites →https://doi.org/10.1038/emboj.2013.189openalex-snapshot

WASH inhibits autophagy through suppression of Beclin 1 ubiquitination

inferredcites →https://doi.org/10.1038/nature11910openalex-snapshot

Autophagosomes form at ER–mitochondria contact sites

inferredcites →https://doi.org/10.1038/ncb1991openalex-snapshot

A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation

inferredcites →https://doi.org/10.1038/ncb2078openalex-snapshot

Plasma membrane contributes to the formation of pre-autophagosomal structures

inferredcites →https://doi.org/10.1038/ncb2152openalex-snapshot

AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1

inferredcites →https://doi.org/10.1038/ncb2708openalex-snapshot

mTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6

inferredcites →https://doi.org/10.1038/ncb2940openalex-snapshot

Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3

inferredcites →https://doi.org/10.1038/ncomms10338openalex-snapshot

The Atg1–kinase complex tethers Atg9-vesicles to initiate autophagy

inferredcites →https://doi.org/10.1038/ncomms12420openalex-snapshot

Autophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles

inferredcites →https://doi.org/10.1038/ncomms15637openalex-snapshot

WIPI3 and WIPI4 β-propellers are scaffolds for LKB1-AMPK-TSC signalling circuits in the control of autophagy

inferredcites →https://doi.org/10.1038/ncomms4920openalex-snapshot

NRBF2 regulates autophagy and prevents liver injury by modulating Atg14L-linked phosphatidylinositol-3 kinase III activity

inferredcites →https://doi.org/10.1038/nrm3696openalex-snapshot

The autophagosome: origins unknown, biogenesis complex

inferredcites →https://doi.org/10.1038/s41467-017-00302-3openalex-snapshot

Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation

inferredcites →https://doi.org/10.1038/s41467-017-00303-2openalex-snapshot

A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B

inferredcites →https://doi.org/10.1038/s41467-018-05254-wopenalex-snapshot

An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure

inferredcites →https://doi.org/10.1038/s41467-019-08335-6openalex-snapshot

LC3/GABARAPs drive ubiquitin-independent recruitment of Optineurin and NDP52 to amplify mitophagy

inferredcites →https://doi.org/10.1038/s41556-019-0274-9openalex-snapshot

Distinct functions of ATG16L1 isoforms in membrane binding and LC3B lipidation in autophagy-related processes

inferredcites →https://doi.org/10.1038/s41580-018-0003-4openalex-snapshot

Mechanism and medical implications of mammalian autophagy

inferredcites →https://doi.org/10.1038/s41580-018-0071-5openalex-snapshot

Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes

inferredcites →https://doi.org/10.1038/s41580-019-0177-4openalex-snapshot

The many functions of ESCRTs

inferredcites →https://doi.org/10.1038/s41586-020-1977-6openalex-snapshot

Phase separation organizes the site of autophagosome formation

inferredcites →https://doi.org/10.1038/s41589-019-0307-5openalex-snapshot

The cholesterol transfer protein GRAMD1A regulates autophagosome biogenesis

inferredcites →https://doi.org/10.1038/s41594-019-0203-4openalex-snapshot

Atg2 mediates direct lipid transfer between membranes for autophagosome formation

inferredcites →https://doi.org/10.1038/sj.emboj.7600203openalex-snapshot

Svp1p defines a family of phosphatidylinositol 3,5‐bisphosphate effectors

inferredcites →https://doi.org/10.1038/sj.emboj.7601623openalex-snapshot

Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4

inferredcites →https://doi.org/10.1038/sj.onc.1208331openalex-snapshot

WIPI-1α (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy

inferredcites →https://doi.org/10.1042/bj20140515openalex-snapshot

NRBF2 regulates macroautophagy as a component of Vps34 Complex I

inferredcites →https://doi.org/10.1073/pnas.1016472108openalex-snapshot

Autophagosome targeting and membrane curvature sensing by Barkor/Atg14(L)

inferredcites →https://doi.org/10.1073/pnas.1100844108openalex-snapshot

Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK

inferredcites →https://doi.org/10.1073/pnas.1316356110openalex-snapshot

The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway

inferredcites →https://doi.org/10.1073/pnas.1523145113openalex-snapshot

PtdIns(4,5)P 2 signaling regulates ATG14 and autophagy

inferredcites →https://doi.org/10.1073/pnas.1603650113openalex-snapshot

Dynamics and architecture of the NRBF2-containing phosphatidylinositol 3-kinase complex I of autophagy

inferredcites →https://doi.org/10.1073/pnas.1717327114openalex-snapshot

AP-4 mediates export of ATG9A from the trans -Golgi network to promote autophagosome formation

inferredcites →https://doi.org/10.1073/pnas.1806727115openalex-snapshot

The Atg2-Atg18 complex tethers pre-autophagosomal membranes to the endoplasmic reticulum for autophagosome formation

inferredcites →https://doi.org/10.1073/pnas.1811874115openalex-snapshot

Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex

inferredcites →https://doi.org/10.1073/pnas.1910854117openalex-snapshot

ER membranes exhibit phase behavior at sites of organelle contact

inferredcites →https://doi.org/10.1074/jbc.272.4.2477openalex-snapshot

Characterization of p150, an Adaptor Protein for the Human Phosphatidylinositol (PtdIns) 3-Kinase

inferredcites →https://doi.org/10.1074/jbc.m112.378109openalex-snapshot

ATG8 Family Proteins Act as Scaffolds for Assembly of the ULK Complex

inferredcites →https://doi.org/10.1074/jbc.m112.411454openalex-snapshot

Atg9 Vesicles Recruit Vesicle-tethering Proteins Trs85 and Ypt1 to the Autophagosome Formation Site

inferredcites →https://doi.org/10.1074/jbc.m115.689646openalex-snapshot

Nutrient-regulated Phosphorylation of ATG13 Inhibits Starvation-induced Autophagy

inferredcites →https://doi.org/10.1074/jbc.m607031200openalex-snapshot

Microtubules Support Production of Starvation-induced Autophagosomes but Not Their Targeting and Fusion with Lysosomes

inferredcites →https://doi.org/10.1074/jbc.m703663200openalex-snapshot

siRNA Screening of the Kinome Identifies ULK1 as a Multidomain Modulator of Autophagy

inferredcites →https://doi.org/10.1074/jbc.m900573200openalex-snapshot

ULK1·ATG13·FIP200 Complex Mediates mTOR Signaling and Is Essential for Autophagy

inferredcites →https://doi.org/10.1074/jbc.r117.810366openalex-snapshot

A molecular perspective of mammalian autophagosome biogenesis

inferredcites →https://doi.org/10.1078/0171-9335-00125openalex-snapshot

Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy

inferredcites →https://doi.org/10.1080/15548627.2015.1034413openalex-snapshot

TipC and the chorea-acanthocytosis protein VPS13A regulate autophagy in Dictyostelium and human HeLa cells

inferredcites →https://doi.org/10.1080/15548627.2015.1076606openalex-snapshot

Autophagy of cytoplasmic bulk cargo does not require LC3

inferredcites →https://doi.org/10.1080/15548627.2015.1091552openalex-snapshot

Autophagosome closure requires membrane scission

inferredcites →https://doi.org/10.1080/15548627.2016.1140293openalex-snapshot

The ULK1 complex mediates MTORC1 signaling to the autophagy initiation machinery via binding and phosphorylating ATG14

inferredcites →https://doi.org/10.1080/15548627.2016.1185576openalex-snapshot

AMPK regulates autophagy by phosphorylating BECN1 at threonine 388

inferredcites →https://doi.org/10.1080/15548627.2016.1226736openalex-snapshot

Characterization of Atg38 and NRBF2, a fifth subunit of the autophagic Vps34/PIK3C3 complex

inferredcites →https://doi.org/10.1080/15548627.2016.1269988openalex-snapshot

MTORC1-mediated NRBF2 phosphorylation functions as a switch for the class III PtdIns3K and autophagy

inferredcites →https://doi.org/10.1080/15548627.2017.1287651openalex-snapshot

ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8

inferredcites →https://doi.org/10.1080/15548627.2017.1320467openalex-snapshot

Autophagy impairment mediated by S-nitrosation of ATG4B leads to neurotoxicity in response to hyperglycemia

inferredcites →https://doi.org/10.1080/15548627.2017.1359381openalex-snapshot

Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial for complex formation

inferredcites →https://doi.org/10.1080/15548627.2018.1437341openalex-snapshot

Delipidation of mammalian Atg8-family proteins by each of the four ATG4 proteases

inferredcites →https://doi.org/10.1080/15548627.2019.1632620openalex-snapshot

GABARAPs and LC3s have opposite roles in regulating ULK1 for autophagy induction

inferredcites →https://doi.org/10.1080/15548627.2019.1639301openalex-snapshot

ESCRT-mediated phagophore sealing during mitophagy

inferredcites →https://doi.org/10.1080/15548627.2019.1659608openalex-snapshot

De novo phosphatidylcholine synthesis is required for autophagosome membrane formation and maintenance during autophagy

inferredcites →https://doi.org/10.1083/jcb.110.6.1923openalex-snapshot

Studies on the mechanisms of autophagy: formation of the autophagic vacuole.

inferredcites →https://doi.org/10.1083/jcb.110.6.1935openalex-snapshot

Studies on the mechanisms of autophagy: maturation of the autophagic vacuole.

inferredcites →https://doi.org/10.1083/jcb.131.3.591openalex-snapshot

Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway.

inferredcites →https://doi.org/10.1083/jcb.147.2.435openalex-snapshot

Formation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast

inferredcites →https://doi.org/10.1083/jcb.151.2.263openalex-snapshot

The Reversible Modification Regulates the Membrane-Binding State of Apg8/Aut7 Essential for Autophagy and the Cytoplasm to Vacuole Targeting Pathway

inferredcites →https://doi.org/10.1083/jcb.151.5.1025openalex-snapshot

Dissection of Autophagosome Biogenesis into Distinct Nucleation and Expansion Steps

inferredcites →https://doi.org/10.1083/jcb.200702115openalex-snapshot

Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease

inferredcites →https://doi.org/10.1083/jcb.200712064openalex-snapshot

FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells

inferredcites →https://doi.org/10.1083/jcb.200803137openalex-snapshot

Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum

inferredcites →https://doi.org/10.1083/jcb.200911141openalex-snapshot

Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L

inferredcites →https://doi.org/10.1083/jcb.200912089openalex-snapshot

An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis

inferredcites →https://doi.org/10.1083/jcb.201002100openalex-snapshot

The dynamic interaction of AMBRA1 with the dynein motor complex regulates mammalian autophagy

inferredcites →https://doi.org/10.1083/jcb.201111079openalex-snapshot

TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes

inferredcites →https://doi.org/10.1083/jcb.201202061openalex-snapshot

Atg9 vesicles are an important membrane source during early steps of autophagosome formation

inferredcites →https://doi.org/10.1083/jcb.201205129openalex-snapshot

Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation

inferredcites →https://doi.org/10.1083/jcb.201605089openalex-snapshot

Fine-tuning of ULK1 mRNA and protein levels is required for autophagy oscillation

inferredcites →https://doi.org/10.1083/jcb.201607039openalex-snapshot

Atg8 family LC3/GABARAP proteins are crucial for autophagosome–lysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation

inferredcites →https://doi.org/10.1083/jcb.201710116openalex-snapshot

Atg9 establishes Atg2-dependent contact sites between the endoplasmic reticulum and phagophores

inferredcites →https://doi.org/10.1083/jcb.201804111openalex-snapshot

Competitive organelle-specific adaptors recruit Vps13 to membrane contact sites

inferredcites →https://doi.org/10.1083/jcb.201804132openalex-snapshot

Genome-wide CRISPR screen identifies TMEM41B as a gene required for autophagosome formation

inferredcites →https://doi.org/10.1083/jcb.201807019openalex-snapshot

VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites

inferredcites →https://doi.org/10.1083/jcb.201809032openalex-snapshot

COPII vesicles contribute to autophagosomal membranes

inferredcites →https://doi.org/10.1083/jcb.201810099openalex-snapshot

Autophagosome maturation: An epic journey from the ER to lysosomes

inferredcites →https://doi.org/10.1083/jcb.201811139openalex-snapshot

ATG2 transports lipids to promote autophagosome biogenesis

inferredcites →https://doi.org/10.1083/jcb.201811173openalex-snapshot

Rab5-dependent autophagosome closure by ESCRT

inferredcites →https://doi.org/10.1083/jcb.201901115openalex-snapshot

ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ

inferredcites →https://doi.org/10.1083/jcb.201902170openalex-snapshot

VPS37A directs ESCRT recruitment for phagophore closure

inferredcites →https://doi.org/10.1083/jcb.202001161openalex-snapshot

Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes

inferredcites →https://doi.org/10.1091/mbc.12.12.3821openalex-snapshot

Cvt18/Gsa12 Is Required for Cytoplasm-to-Vacuole Transport, Pexophagy, and Autophagy inSaccharomyces cerevisiaeandPichia pastoris

inferredcites →https://doi.org/10.1091/mbc.e03-10-0732openalex-snapshot

PtdIns-specific MPR Pathway Association of a Novel WD40 Repeat Protein, WIPI49

inferredcites →https://doi.org/10.1091/mbc.e07-12-1292openalex-snapshot

Atg8 Controls Phagophore Expansion during Autophagosome Formation

inferredcites →https://doi.org/10.1091/mbc.e08-03-0312openalex-snapshot

An Atg4B Mutant Hampers the Lipidation of LC3 Paralogues and Causes Defects in Autophagosome Closure

inferredcites →https://doi.org/10.1091/mbc.e08-12-1248openalex-snapshot

Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy

inferredcites →https://doi.org/10.1091/mbc.e08-12-1249openalex-snapshot

ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery

inferredcites →https://doi.org/10.1091/mbc.e11-09-0746openalex-snapshot

Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy

inferredcites →https://doi.org/10.1091/mbc.e11-09-0785openalex-snapshot

Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets

inferredcites →https://doi.org/10.1091/mbc.e13-07-0381openalex-snapshot

ER exit sites are physical and functional core autophagosome biogenesis components

inferredcites →https://doi.org/10.1093/emboj/19.17.4577openalex-snapshot

Localization of phosphatidylinositol 3‐phosphate in yeast and mammalian cells

inferredcites →https://doi.org/10.1093/emboj/20.21.5971openalex-snapshot

The pre‐autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation

inferredcites →https://doi.org/10.1111/j.1600-0854.2010.01034.xopenalex-snapshot

Modulation of Local PtdIns3P Levels by the PI Phosphatase MTMR3 Regulates Constitutive Autophagy

inferredcites →https://doi.org/10.1111/tra.12581openalex-snapshot

Vacuole membrane protein 1 marks endoplasmic reticulum subdomains enriched in phospholipid synthesizing enzymes and is required for phosphoinositide distribution

inferredcites →https://doi.org/10.1111/tra.12640openalex-snapshot

TRAPPC11 functions in autophagy by recruiting ATG2B‐WIPI4/WDR45 to preautophagosomal membranes

inferredcites →https://doi.org/10.1126/science.aaf6136openalex-snapshot

The ATG conjugation systems are important for degradation of the inner autophagosomal membrane

inferredcites →https://doi.org/10.1128/jvi.01341-19openalex-snapshot

COPII Vesicle Transport Is Required for Rotavirus NSP4 Interaction with the Autophagy Protein LC3 II and Trafficking to Viroplasms

inferredcites →https://doi.org/10.1128/mcb.01082-08openalex-snapshot

Kinase-Inactivated ULK Proteins Inhibit Autophagy via Their Conserved C-Terminal Domains Using an Atg13-Independent Mechanism

inferredcites →https://doi.org/10.1146/annurev-biochem-061516-044820openalex-snapshot

Mechanisms of Autophagy Initiation

inferredcites →https://doi.org/10.1146/annurev-cellbio-092910-154005openalex-snapshot

The Role of Atg Proteins in Autophagosome Formation

inferredcites →https://doi.org/10.1159/000350326openalex-snapshot

Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila

inferredcites →https://doi.org/10.1159/000373980openalex-snapshot

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

inferredcites →https://doi.org/10.1186/s13024-016-0141-0openalex-snapshot

ULK1-mediated phosphorylation of ATG14 promotes autophagy and is impaired in Huntington’s disease models

inferredcites →https://doi.org/10.1194/jlr.m046359openalex-snapshot

Lipid droplet and early autophagosomal membrane targeting of Atg2A and Atg14L in human tumor cells

inferredcites →https://doi.org/10.1242/jcs.03172openalex-snapshot

Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes

inferredcites →https://doi.org/10.1242/jcs.093203openalex-snapshot

AP1 is essential for generation of autophagosomes from trans-Golgi network

inferredcites →https://doi.org/10.1242/jcs.122960openalex-snapshot

Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1242/jcs.132415openalex-snapshot

Dynamic association of the ULK1 complex with omegasomes during autophagy induction

inferredcites →https://doi.org/10.1242/jcs.141036openalex-snapshot

Membrane dynamics in autophagosome biogenesis

inferredcites →https://doi.org/10.1242/jcs.146258openalex-snapshot

WIPI proteins: essential PtdIns3 P effectors at the nascent autophagosome

inferredcites →https://doi.org/10.1242/jcs.156034openalex-snapshot

Ultrastructural analysis of autophagosome organization using mammalian autophagy-deficient cells

inferredcites →https://doi.org/10.1242/jcs.194373openalex-snapshot

Atg20- and Atg24-family proteins promote organelle autophagy in fission yeast

inferredcites →https://doi.org/10.1242/jcs.196196openalex-snapshot

Atg9A trafficking through the recycling endosomes is required for autophagosome formation

inferredcites →https://doi.org/10.1247/csf.20.465openalex-snapshot

Analysis of the Membrane Structures Involved in Autophagy in Yeast by Freeze-Replica Method.

inferredcites →https://doi.org/10.1371/journal.pbio.2007044openalex-snapshot

CRISPR screening using an expanded toolkit of autophagy reporters identifies TMEM41B as a novel autophagy factor

inferredcites →https://doi.org/10.1371/journal.pbio.3000377openalex-snapshot

Atg11 tethers Atg9 vesicles to initiate selective autophagy

inferredcites →https://doi.org/10.1371/journal.pgen.1003007openalex-snapshot

Regulation of ATG4B Stability by RNF5 Limits Basal Levels of Autophagy and Influences Susceptibility to Bacterial Infection

inferredcites →https://doi.org/10.1371/journal.pone.0115357openalex-snapshot

Membrane Morphology Is Actively Transformed by Covalent Binding of the Protein Atg8 to PE-Lipids

inferredcites →https://doi.org/10.1371/journal.pone.0184909openalex-snapshot

PI3K-C2α knockdown decreases autophagy and maturation of endocytic vesicles

inferredcites →https://doi.org/10.15252/embj.201592864openalex-snapshot

PAQR3 controls autophagy by integrating AMPK signaling to enhance ATG14L‐associated PI3K activity

inferredcites →https://doi.org/10.15252/embj.201694401openalex-snapshot

The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy

inferredcites →https://doi.org/10.15252/embj.201695189openalex-snapshot

Autophagosome formation is initiated at phosphatidylinositol synthase‐enriched ER subdomains

inferredcites →https://doi.org/10.15252/embj.201796697openalex-snapshot

Molecular definitions of autophagy and related processes

inferredcites →https://doi.org/10.15252/embr.201744559openalex-snapshot

Remodeling of ER‐exit sites initiates a membrane supply pathway for autophagosome biogenesis

inferredcites →https://doi.org/10.15252/embr.201744837openalex-snapshot

SNX18 regulates ATG9A trafficking from recycling endosomes by recruiting Dynamin‐2

inferredcites →https://doi.org/10.15252/embr.201845889openalex-snapshot

TMEM41B is a novel regulator of autophagy and lipid mobilization

inferredcites →https://doi.org/10.15252/embr.201948317openalex-snapshot

TBK1‐mediated phosphorylation of LC3C and GABARAP‐L2 controls autophagosome shedding by ATG4 protease

inferredcites →https://doi.org/10.15252/embr.201948412openalex-snapshot

A conserved ATG2‐GABARAP family interaction is critical for phagophore formation

inferredcites →https://doi.org/10.15698/mic2016.12.546openalex-snapshot

Autophagy: machinery and regulation

inferredcites →https://doi.org/10.18632/oncotarget.11083openalex-snapshot

O-GlcNAcylation of ATG4B positively regulates autophagy by increasing its hydroxylase activity

inferredcites →https://doi.org/10.18632/oncotarget.22714openalex-snapshot

Atg4 in autophagosome biogenesis

inferredcites →https://doi.org/10.4161/auto.1.2.1840openalex-snapshot

Atg9 Cycles Between Mitochondria and the Pre-Autophagosomal Structure in Yeasts

inferredcites →https://doi.org/10.4161/auto.25529openalex-snapshot

Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site

inferredcites →https://doi.org/10.4161/auto.34396openalex-snapshot

The yeast autophagy protease Atg4 is regulated by thioredoxin

showing the first 200 of 207

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Intricacies of Lipid Supply in Autophagic Membrane Expansion

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A Sonication‐Activated Valence‐Variable Sono‐Sensitizer/Catalyst for Autography Inhibition/Ferroptosis‐Induced Tumor Nanotherapy

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A Sonication‐Activated Valence‐Variable Sono‐Sensitizer/Catalyst for Autography Inhibition/Ferroptosis‐Induced Tumor Nanotherapy

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Expanding the view of the molecular mechanisms of autophagy pathway

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No energy, no autophagy—Mechanisms and therapeutic implications of autophagic response energy requirements

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Mechanisms of Autophagy in Ineffective Reperfusion After Ischemic Stroke

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Silencing LsAtg8 reduces female fecundity and elevates Wolbachia density in embryos of the rice planthopper Laodelphax striatellus

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Natural products targeting macroautophagy signaling in hepatocellular carcinoma therapy: Recent evidence and perspectives

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Studying Autophagy in Microglia: Overcoming the Obstacles

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Methods to Assess Autophagic Activity in Dictyostelium

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Assays for Monitoring Autophagy in Stem Cells

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Autophagy and Reactive Oxygen Species in Cancer: An Introduction

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Autophagy-Targeted Nanoparticles for the Treatment of Cancer

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The Source of Membrane During Autophagy and the Early Steps in Autophagosome Formation

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Mitophagy Responds to the Environmental Temperature and Regulates Mitochondrial Mass in Adipose Tissues

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AMPK: a key regulator of energy stress and calcium-induced autophagy

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Autophagy impairs the sensitivity of Ewing sarcoma cells to PARP inhibitors

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Periodontopathogen-Related Cell Autophagy—A Double-Edged Sword

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Targeting autophagy in oral squamous cell carcinoma chemoresistance: molecular mechanisms, therapeutic strategies, and emerging nanotherapeutic approaches

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Autophagic Pathway on GABARAP Involved in GABAA Receptor Trafficking

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Deficiency of RAB39B Activates ER Stress-Induced Pro-apoptotic Pathway and Causes Mitochondrial Dysfunction and Oxidative Stress in Dopaminergic Neurons by Impairing Autophagy and Upregulating α-Synuclein

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C9orf72-Associated Dipeptide Repeat Expansions Perturb ER-Golgi Vesicular Trafficking, Inducing Golgi Fragmentation and ER Stress, in ALS/FTD

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Reinventing the Penumbra — the Emerging Clockwork of a Multi-modal Mechanistic Paradigm

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Lipids and membrane-associated proteins in autophagy

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Metabolic aspects of canonical versus noncanonical autophagy

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Overview of noncanonical autophagy

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Lipids in membrane formation for autophagosomes and autophagy induction

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Autophagy and the inflammasome

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Molecular dynamics of autophagy in cancer metabolism

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Historical context and the evolution of exosome research

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Unraveling the interplay of glycolysis, lactylation, and autophagy

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In vitro methods for measuring lipid binding, transfer and competitive displacement reactions by peripheral membrane proteins

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Targeting autophagy and beyond: Deconvoluting the complexity of Beclin-1 from biological function to cancer therapy

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Regulated cell death in systemic lupus erythematosus: Key pathways and targeted therapies

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Lipid-autophagy crosstalk in glioblastoma: A context-dependent stress-adaptation interface under temozolomide pressure

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Phosphoinositides: Functions in autophagy-related stress responses

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Phosphoinositide transport and metabolism at membrane contact sites

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Ceramide regulation of autophagy: A biophysical approach

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Molecular and mesoscopic geometries in autophagosome generation. A review

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Chemoproteomics reveals arctigenin as a phagophore-closure blocker via targeting ESCRT-I subunit VPS28

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Autophagy in sarcopenia: Possible mechanisms and novel therapies

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Skeletal and dental tissue mineralization: The potential role of the endoplasmic reticulum/Golgi complex and the endolysosomal and autophagic transport systems

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Growing thin — How bulk lipid transport drives expansion of the autophagosome membrane but not of its lumen

inferred← citeshttps://doi.org/10.1016/j.ceb.2024.102377openalex-snapshot

Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow

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Advances in mitophagy initiation mechanisms

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Hyaluronic acid-coated ROS-responsive mesoporous organosilica nanoparticles for enhanced curcumin delivery and redox remodeling in liver fibrosis

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Mammalian hybrid pre-autophagosomal structure HyPAS generates autophagosomes

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Mechanism of lipid transfer by bridge-like protein VPS13A and the scramblase XK

inferred← citeshttps://doi.org/10.1016/j.celrep.2023.112943openalex-snapshot

Autophagy collaborates with apoptosis pathways to control oligodendrocyte number

inferred← citeshttps://doi.org/10.1016/j.celrep.2024.114293openalex-snapshot

Pain hypersensitivity is dependent on autophagy protein Beclin 1 in males but not females

inferred← citeshttps://doi.org/10.1016/j.conb.2022.102554openalex-snapshot

Organization of the autophagy pathway in neurons

inferred← citeshttps://doi.org/10.1016/j.cophys.2022.100592openalex-snapshot

Role of autophagy in the eye: from physiology to disease

inferred← citeshttps://doi.org/10.1016/j.cub.2022.11.002openalex-snapshot

Orchestration of selective autophagy by cargo receptors

inferred← citeshttps://doi.org/10.1016/j.devcel.2019.01.027openalex-snapshot

Phosphorylation of Syntaxin 17 by TBK1 Controls Autophagy Initiation

inferred← citeshttps://doi.org/10.1016/j.devcel.2023.05.009openalex-snapshot

LC3B is lipidated to large lipid droplets during prolonged starvation for noncanonical autophagy

inferred← citeshttps://doi.org/10.1016/j.devcel.2023.08.016openalex-snapshot

Mammalian autophagosomes form from finger-like phagophores

inferred← citeshttps://doi.org/10.1016/j.devcel.2023.11.006openalex-snapshot

An Arabidopsis Rab18 GTPase promotes autophagy by tethering ATG18a to the ER in response to nutrient starvation

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Accumulation of autophagosomes in aging human photoreceptor cell synapses

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ATG9A as a potential diagnostic marker of intervertebral disc degeneration: Inferences from experiments and bioinformatics analysis incorporating sc-RNA-seq data

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.05.129openalex-snapshot

Autophagy protein LC3C binding to phospholipid and interaction with lipid membranes

inferred← citeshttps://doi.org/10.1016/j.immuni.2021.01.018openalex-snapshot

Autophagy in inflammation, infection, and immunometabolism

inferred← citeshttps://doi.org/10.1016/j.isci.2024.111268openalex-snapshot

Autophagy in reproduction and pregnancy-associated diseases

inferred← citeshttps://doi.org/10.1016/j.isci.2025.112801openalex-snapshot

Erythrabyssin ll is identified as a late-stage autophagy inhibitor reversing chemoresistance and promoting apoptosis in ovarian cancer

inferred← citeshttps://doi.org/10.1016/j.isci.2026.115056openalex-snapshot

Loss of DDI2 rewires proteostasis through CCN1-driven compensatory autophagy

inferred← citeshttps://doi.org/10.1016/j.isci.2026.117518openalex-snapshot

PP2A and CDK16 antagonistically regulate WIPI2B phosphorylation and neuronal autophagosome biogenesis

inferred← citeshttps://doi.org/10.1016/j.jbc.2022.101573openalex-snapshot

Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway

inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102673openalex-snapshot

Brain-derived neurotrophic factor stimulates the retrograde pathway for axonal autophagy

inferred← citeshttps://doi.org/10.1016/j.jbc.2025.110391openalex-snapshot

The human autophagy-initiating complexes ULK1C and PI3KC3-C1

inferred← citeshttps://doi.org/10.1016/j.jia.2025.03.022openalex-snapshot

CaBBX9, an interaction partner of autophagy-related protein CaATG8c, negatively regulates the heat tolerance of pepper

inferred← citeshttps://doi.org/10.1016/j.jmb.2024.168691openalex-snapshot

Phospholipid Supply for Autophagosome Biogenesis

inferred← citeshttps://doi.org/10.1016/j.jmb.2025.169105openalex-snapshot

The Life and Times of Brain Autophagic Vesicles

inferred← citeshttps://doi.org/10.1016/j.jmb.2025.169219openalex-snapshot

Autophagy Dysfunction and Neurodegeneration: Where Does It Go Wrong?

inferred← citeshttps://doi.org/10.1016/j.jmb.2025.169288openalex-snapshot

ATG9 Not Just an Autophagy Related Protein

inferred← citeshttps://doi.org/10.1016/j.matbio.2021.01.001openalex-snapshot

Amino acid sensory complex proteins in mTORC1 and macroautophagy regulation

inferred← citeshttps://doi.org/10.1016/j.medp.2023.100004openalex-snapshot

Perspectives of autophagy-tethering compounds (ATTECs) in drug discovery

inferred← citeshttps://doi.org/10.1016/j.molcel.2019.01.041openalex-snapshot

The Cargo Receptor NDP52 Initiates Selective Autophagy by Recruiting the ULK Complex to Cytosol-Invading Bacteria

inferred← citeshttps://doi.org/10.1016/j.molcel.2022.03.023openalex-snapshot

Autophagy in cancer cell remodeling and quality control

inferred← citeshttps://doi.org/10.1016/j.molcel.2022.10.017openalex-snapshot

ATG9A and ATG2A form a heteromeric complex essential for autophagosome formation

inferred← citeshttps://doi.org/10.1016/j.molcel.2023.04.021openalex-snapshot

Unconventional initiation of PINK1/Parkin mitophagy by Optineurin

inferred← citeshttps://doi.org/10.1016/j.molcel.2023.04.026openalex-snapshot

Metamorphic proteins at the basis of human autophagy initiation and lipid transfer

inferred← citeshttps://doi.org/10.1016/j.ortho.2025.101076openalex-snapshot

Expression of autophagy and apoptosis during orthodontic tooth movement alveolar bone remodeling in rats with varied periodontal conditions

inferred← citeshttps://doi.org/10.1016/j.pbiomolbio.2023.10.002openalex-snapshot

Growth or death? Control of cell destiny by mTOR and autophagy pathways

inferred← citeshttps://doi.org/10.1016/j.phrs.2025.108023openalex-snapshot

Crosstalk between lipid droplets and autophagy in cancer: A nexus for therapeutic targeting

inferred← citeshttps://doi.org/10.1016/j.plipres.2026.101384openalex-snapshot

Nature, functions and trafficking of membrane lipids to support autophagosome formation in plant cells

inferred← citeshttps://doi.org/10.1016/j.redox.2025.103852openalex-snapshot

An emerging role for cysteine-mediated redox signaling in aging

inferred← citeshttps://doi.org/10.1016/j.taap.2024.116890openalex-snapshot

Crosstalk between autophagy and inflammasomes in ricin-induced inflammatory injury

inferred← citeshttps://doi.org/10.1016/j.tcb.2025.01.002openalex-snapshot

Endoplasmic reticulum (ER) protein degradation by ER-associated degradation and ER-phagy

inferred← citeshttps://doi.org/10.1016/j.theriogenology.2022.10.018openalex-snapshot

Autophagy phenomenon in mice ovaries following transplantation

inferred← citeshttps://doi.org/10.1016/j.tips.2023.02.003openalex-snapshot

Recent advances in targeting autophagy in cancer

inferred← citeshttps://doi.org/10.1016/j.yexmp.2025.104989openalex-snapshot

The interplay involving oxidative stress and autophagy: Mechanisms, implications, and therapeutic opportunities

inferred← citeshttps://doi.org/10.1016/j.yjmcc.2021.12.006openalex-snapshot

The role of autophagy in death of cardiomyocytes

inferred← citeshttps://doi.org/10.1038/s12276-024-01337-5openalex-snapshot

Interplay between membranes and biomolecular condensates in the regulation of membrane-associated cellular processes

inferred← citeshttps://doi.org/10.1038/s41392-025-02501-7openalex-snapshot

The role of ER-associated degradation and ER-phagy in health and disease

inferred← citeshttps://doi.org/10.1038/s41419-021-04335-xopenalex-snapshot

CaMKK2 facilitates Golgi-associated vesicle trafficking to sustain cancer cell proliferation

inferred← citeshttps://doi.org/10.1038/s41419-022-04722-yopenalex-snapshot

TMEM189 negatively regulates the stability of ULK1 protein and cell autophagy

inferred← citeshttps://doi.org/10.1038/s41419-025-08093-yopenalex-snapshot

TM9SF1 drives the lipophagic flux via AMPK-ULK1 signaling to sustain metabolic fitness in HER2-positive breast cancer

inferred← citeshttps://doi.org/10.1038/s41421-023-00583-7openalex-snapshot

Cell type-specific NRBF2 orchestrates autophagic flux and adult hippocampal neurogenesis in chronic stress-induced depression

inferred← citeshttps://doi.org/10.1038/s41421-024-00659-yopenalex-snapshot

ANKFY1 bridges ATG2A-mediated lipid transfer from endosomes to phagophores

inferred← citeshttps://doi.org/10.1038/s41467-021-26999-xopenalex-snapshot

The autophagy protein ATG9A enables lipid mobilization from lipid droplets

inferred← citeshttps://doi.org/10.1038/s41467-023-37016-8openalex-snapshot

De novo lipogenesis fuels adipocyte autophagosome and lysosome membrane dynamics

inferred← citeshttps://doi.org/10.1038/s41467-023-37185-6openalex-snapshot

The plant unique ESCRT component FREE1 regulates autophagosome closure

inferred← citeshttps://doi.org/10.1038/s41467-023-40530-4openalex-snapshot

A conserved membrane curvature-generating protein is crucial for autophagosome formation in fission yeast

inferred← citeshttps://doi.org/10.1038/s41467-023-41618-7openalex-snapshot

Tumor-intrinsic expression of the autophagy gene Atg16l1 suppresses anti-tumor immunity in colorectal cancer

inferred← citeshttps://doi.org/10.1038/s41467-024-49485-6openalex-snapshot

Arabidopsis CaLB1 undergoes phase separation with the ESCRT protein ALIX and modulates autophagosome maturation

inferred← citeshttps://doi.org/10.1038/s41467-025-57985-2openalex-snapshot

Lipid packing and cholesterol content regulate membrane wetting and remodeling by biomolecular condensates

inferred← citeshttps://doi.org/10.1038/s41467-026-69025-8openalex-snapshot

Supercharging-enhanced nDIA-MS enables global profiling of drug-induced proteome solubility shifts

inferred← citeshttps://doi.org/10.1038/s41467-026-71237-xopenalex-snapshot

Nucleophagy is promoted by two autophagy receptors and inhibited by chromatin-nuclear envelope tethering in fission yeast

inferred← citeshttps://doi.org/10.1038/s41467-026-71551-4openalex-snapshot

Translation in proximity to forming autophagosomes during sustained autophagy

inferred← citeshttps://doi.org/10.1038/s41467-026-75742-xopenalex-snapshot

Lipid-manager autophagy proteins ATG2 and ATG9 regulate extracellular vesicle secretion via amphisome biogenesis and cell lipidome modulation

inferred← citeshttps://doi.org/10.1038/s41467-026-76135-wopenalex-snapshot

A GABARAP−PtdIns3K-C1 positive feedback loop at the heart of the phagophore nucleation

inferred← citeshttps://doi.org/10.1038/s41467-026-76615-zopenalex-snapshot

Inhibition of RhoA-mediated secretory autophagy in megakaryocytes mitigates myelofibrosis in mice

inferred← citeshttps://doi.org/10.1038/s41467-026-77368-5openalex-snapshot

A lipid transfer-dependent feedback loop activates ATG9A compartments in autophagy initiation

inferred← citeshttps://doi.org/10.1038/s41556-021-00669-yopenalex-snapshot

Autophagosome biogenesis comes out of the black box

inferred← citeshttps://doi.org/10.1038/s41556-025-01612-1openalex-snapshot

A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope

inferred← citeshttps://doi.org/10.1038/s41556-025-01712-yopenalex-snapshot

Reconstitution of BNIP3/NIX-mitophagy initiation reveals hierarchical flexibility of the autophagy machinery

inferred← citeshttps://doi.org/10.1038/s41574-021-00551-9openalex-snapshot

Autophagy in metabolic disease and ageing

inferred← citeshttps://doi.org/10.1038/s41580-025-00873-wopenalex-snapshot

Lysosomal membrane homeostasis and its importance in physiology and disease

inferred← citeshttps://doi.org/10.1038/s41580-026-00961-5openalex-snapshot

Phase separation across membranes and condensates in cell organization and function

inferred← citeshttps://doi.org/10.1038/s41580-026-01012-9openalex-snapshot

Regulation and roles of mammalian mitophagy

inferred← citeshttps://doi.org/10.1038/s41594-024-01300-yopenalex-snapshot

ATG16L1 induces the formation of phagophore-like membrane cups

inferred← citeshttps://doi.org/10.1038/s41594-024-01376-6openalex-snapshot

Structural basis for lipid transfer by the ATG2A–ATG9A complex

inferred← citeshttps://doi.org/10.1038/s41594-025-01546-0openalex-snapshot

Recruitment of Atg1 to the phagophore by Atg8 orchestrates autophagy machineries

inferred← citeshttps://doi.org/10.1038/s41598-025-18016-8openalex-snapshot

A nile red fluorescence assay for LC3 autophagy protein binding to lipid bilayers

inferred← citeshttps://doi.org/10.1038/s42003-024-06026-7openalex-snapshot

Identification of membrane curvature sensing motifs essential for VPS37A phagophore recruitment and autophagosome closure

inferred← citeshttps://doi.org/10.1038/s42003-025-08877-0openalex-snapshot

CPT2 inhibition enhances selective autophagy and proliferation in colorectal cancer via GPAT4-dependent glycerophospholipid biosynthesis

inferred← citeshttps://doi.org/10.1038/s42003-026-10067-5openalex-snapshot

Nrf1 coordinates proteasome activity and autophagy to maintain cardiac proteostasis

inferred← citeshttps://doi.org/10.1038/s44318-024-00280-5openalex-snapshot

Recruitment of autophagy initiator TAX1BP1 advances aggrephagy from cargo collection to sequestration

inferred← citeshttps://doi.org/10.1038/s44318-025-00436-xopenalex-snapshot

Autophagosomes anchor an AKAP11-dependent regulatory checkpoint that shapes neuronal PKA signaling

inferred← citeshttps://doi.org/10.1038/s44318-025-00543-9openalex-snapshot

BLTP3A is associated with membranes of the late endocytic pathway and is an effector of CASM

inferred← citeshttps://doi.org/10.1038/s44318-025-00615-wopenalex-snapshot

Mechanism of autophagy initiation by transmembrane selective autophagy receptors

inferred← citeshttps://doi.org/10.1038/s44318-025-00686-9openalex-snapshot

MYO5A-mediated stabilization promotes the acquisition of fusion competence in sealed autophagosomes

inferred← citeshttps://doi.org/10.1039/d2cs00624copenalex-snapshot

Emerging degrader technologies engaging lysosomal pathways

inferred← citeshttps://doi.org/10.1042/bcj20250148openalex-snapshot

Cutting edge: ESCRT-mediated phagophore closure in mammals

inferred← citeshttps://doi.org/10.1042/bst20230897openalex-snapshot

PROPPINs and membrane fission in the endo-lysosomal system

inferred← citeshttps://doi.org/10.1042/ns20210063openalex-snapshot

Keeping synapses in shape: degradation pathways in the healthy and aging brain

inferred← citeshttps://doi.org/10.1055/a-2153-9258openalex-snapshot

Autophagy and Exercise: Current Insights and Future Research Directions

inferred← citeshttps://doi.org/10.1073/pnas.2209823119openalex-snapshot

In situ structural analysis reveals membrane shape transitions during autophagosome formation

inferred← citeshttps://doi.org/10.1073/pnas.2221712120openalex-snapshot

In situ snapshots along a mammalian selective autophagy pathway

inferred← citeshttps://doi.org/10.1073/pnas.2321579121openalex-snapshot

Membrane nanotubes transform into double-membrane sheets at condensate droplets

inferred← citeshttps://doi.org/10.1073/pnas.2517469122openalex-snapshot

ATG2 is a triglyceride transfer protein

inferred← citeshttps://doi.org/10.1073/pnas.2523465123openalex-snapshot

ER membrane receptors engage core autophagy machinery to initiate ER-phagy

inferred← citeshttps://doi.org/10.1080/15548627.2021.1933742openalex-snapshot

Autophagy in metabolism and quality control: opposing, complementary or interlinked functions?

inferred← citeshttps://doi.org/10.1080/15548627.2021.1953262openalex-snapshot

A Dictyostelium model for BPAN disease reveals a functional relationship between the WDR45/WIPI4 homolog Wdr45l and Vmp1 in the regulation of autophagy-associated PtdIns3P and ER stress

inferred← citeshttps://doi.org/10.1080/15548627.2021.1953820openalex-snapshot

SQSTM1/p62 droplet -mediated autophagosome formation:insights into Huntington disease

inferred← citeshttps://doi.org/10.1080/15548627.2021.1997305openalex-snapshot

Post-transcriptional regulation ofATG1is a critical node that modulates autophagy during distinct nutrient stresses

inferred← citeshttps://doi.org/10.1080/15548627.2022.2065617openalex-snapshot

Autophagy profiling in single cells with open source CellProfiler-based image analysis

inferred← citeshttps://doi.org/10.1080/15548627.2022.2067383openalex-snapshot

Crosstalk between cilia and autophagy: implication for human diseases

inferred← citeshttps://doi.org/10.1080/15548627.2022.2070331openalex-snapshot

Multifaceted roles of TAX1BP1 in autophagy

inferred← citeshttps://doi.org/10.1080/15548627.2022.2084884openalex-snapshot

Proteasomal inhibition preferentially stimulates lysosome activity relative to autophagic flux in primary astrocytes

inferred← citeshttps://doi.org/10.1080/15548627.2023.2236485openalex-snapshot

Aging Differentially Affects Axonal Autophagosome Formation and Maturation

inferred← citeshttps://doi.org/10.1080/15548627.2023.2275905openalex-snapshot

ATG9B is a tissue-specific homotrimeric lipid scramblase that can compensate for ATG9A

inferred← citeshttps://doi.org/10.1080/15548627.2024.2375785openalex-snapshot

GORASP2 promotes phagophore closure and autophagosome maturation into autolysosomes

inferred← citeshttps://doi.org/10.1080/15548627.2024.2384349openalex-snapshot

Emerging roles of ATG9/ATG9A in autophagy: implications for cell and neurobiology

inferred← citeshttps://doi.org/10.1080/15548627.2024.2443300openalex-snapshot

Blocking autophagosome closure manifests the roles of mammalian Atg8-family proteins in phagophore formation and expansion during nutrient starvation

inferred← citeshttps://doi.org/10.1080/15548627.2024.2447206openalex-snapshot

The ER protein CANX (calnexin)-mediated autophagy protects against alzheimer disease

inferred← citeshttps://doi.org/10.1080/15548627.2025.2551678openalex-snapshot

Reconstitution of autophagic-like membrane tethering reveals that Atg11 can bind and cluster vesicles on cargo mimetics

inferred← citeshttps://doi.org/10.1080/15548627.2025.2559728openalex-snapshot

Pneumolysin-dependent and independent non-canonical autophagy processes mediate host defense against pneumococcal infection

inferred← citeshttps://doi.org/10.1080/15548627.2025.2581217openalex-snapshot

Autophagy and mitophagy at the synapse and beyond: implications for learning, memory and neurological disorders

inferred← citeshttps://doi.org/10.1080/15548627.2026.2636096openalex-snapshot

Autophagy as a therapeutic linchpin in metabolic diseases and obesity-associated diabetes

inferred← citeshttps://doi.org/10.1080/15548627.2026.2657543openalex-snapshot

In situ architecture of developmentally programmed mitophagy reveals ER-phagophore membrane continuity

inferred← citeshttps://doi.org/10.1080/15548627.2026.2672699openalex-snapshot

S -palmitoylation of ATG4B facilitates the deconjugation of LC3-II to promote autophagy

inferred← citeshttps://doi.org/10.1080/27694127.2022.2101335openalex-snapshot

Evaluating Autophagy in Preimplantation Embryos

inferred← citeshttps://doi.org/10.1080/27694127.2023.2179287openalex-snapshot

External stimulation induces the secretion of autophagosome-like vesicles by B cells

inferred← citeshttps://doi.org/10.1080/27694127.2023.2194620openalex-snapshot

A novel autophagy inhibitor, bTBT, disturbs autophagosome formation

inferred← citeshttps://doi.org/10.1080/27694127.2023.2256599openalex-snapshot

Improved volume CLEM revealed that aberrant phagophores and RB1CC1/FIP200-containing clusters appear surround SQSTM1/p62 aggregates in Atg9a -deficient cells

inferred← citeshttps://doi.org/10.1080/27694127.2025.2571940openalex-snapshot

Targeting macroautophagy to combat neurodegenerative disease: strategies and considerations

inferred← citeshttps://doi.org/10.1083/jcb.202004062openalex-snapshot

Liquid–liquid phase separation in autophagy

inferred← citeshttps://doi.org/10.1083/jcb.202006007openalex-snapshot

Stress eating: Autophagy targets nuclear pore complexes

inferred← citeshttps://doi.org/10.1083/jcb.202009128openalex-snapshot

STING induces LC3B lipidation onto single-membrane vesicles via the V-ATPase and ATG16L1-WD40 domain

inferred← citeshttps://doi.org/10.1083/jcb.202012058openalex-snapshot

Mechanisms of nonvesicular lipid transport

inferred← citeshttps://doi.org/10.1083/jcb.202103030openalex-snapshot

Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome

inferred← citeshttps://doi.org/10.1083/jcb.202103175openalex-snapshot

Intracellular wetting mediates contacts between liquid compartments and membrane-bound organelles

inferred← citeshttps://doi.org/10.1083/jcb.202203139openalex-snapshot

Plant autophagosomes mature into amphisomes prior to their delivery to the central vacuole

inferred← citeshttps://doi.org/10.1083/jcb.202205123openalex-snapshot

Quality control mechanisms that protect nuclear envelope identity and function

inferred← citeshttps://doi.org/10.1083/jcb.202205135openalex-snapshot

ER as master regulator of membrane trafficking and organelle function

inferred← citeshttps://doi.org/10.1083/jcb.202211039openalex-snapshot

Parallel phospholipid transfer by Vps13 and Atg2 determines autophagosome biogenesis dynamics

inferred← citeshttps://doi.org/10.1083/jcb.202306150openalex-snapshot

Transcription factor Nrf1 regulates proteotoxic stress-induced autophagy

inferred← citeshttps://doi.org/10.1083/jcb.202310005openalex-snapshot

Regulation of proteostasis and innate immunity via mitochondria-nuclear communication

inferred← citeshttps://doi.org/10.1083/jcb.202404009openalex-snapshot

SNX10 functions as a modulator of piecemeal mitophagy and mitochondrial bioenergetics

inferred← citeshttps://doi.org/10.1091/mbc.e22-07-0279openalex-snapshot

PI(3)P and DFCP1 regulate the biogenesis of lipid droplets

inferred← citeshttps://doi.org/10.1091/mbc.e22-09-0432openalex-snapshot

CCPG1 recognizes endoplasmic reticulum luminal proteins for selective ER-phagy

inferred← citeshttps://doi.org/10.1091/mbc.e25-07-0312openalex-snapshot

Sex does not influence neuronal autophagosome biogenesis throughout aging in mice

inferred← citeshttps://doi.org/10.1093/jb/mvae042openalex-snapshot

Comprehensive analysis of non-selective and selective autophagy in yeast atg mutants and characterization of autophagic activity in the absence of the Atg8 conjugation system

inferred← citeshttps://doi.org/10.1093/jb/mvaf073openalex-snapshot

New insights into the essentiality of core autophagy factors revealed by comprehensive analysis

inferred← citeshttps://doi.org/10.1093/lifemedi/lnac043openalex-snapshot

Manipulating autophagic degradation in human diseases: from mechanisms to interventions

inferred← citeshttps://doi.org/10.1093/ndt/gfad024openalex-snapshot

Autophagy and podocytopathy

inferred← citeshttps://doi.org/10.1093/pcp/pcab045openalex-snapshot

ESCRT Is a Great Sealer: Non-Endosomal Function of the ESCRT Machinery in Membrane Repair and Autophagy

inferred← citeshttps://doi.org/10.1101/2020.07.07.191189openalex-snapshot

FIP200 organizes the autophagy machinery at p62-ubiquitin condensates beyond activation of the ULK1 kinase

inferred← citeshttps://doi.org/10.1101/2022.05.25.493413openalex-snapshot

De novo lipogenesis fuels adipocyte autophagosome membrane dynamics

inferred← citeshttps://doi.org/10.1101/2022.08.08.503181openalex-snapshot

BDNF stimulates the retrograde pathway for axonal autophagy

inferred← citeshttps://doi.org/10.1101/2022.08.27.505553openalex-snapshot

Aging Differentially Affects Axonal Autophagosome Formation and Maturation

inferred← citeshttps://doi.org/10.1101/2022.10.27.514035openalex-snapshot

Membrane curvature-generating proteins crucial for autophagosome formation

inferred← citeshttps://doi.org/10.1101/2022.11.01.514784openalex-snapshot

Curvature Sensing and Membrane Remodeling of the VPS37A N-terminal Domain during Autophagy

inferred← citeshttps://doi.org/10.1101/2023.06.29.547114openalex-snapshot

Transcription factor Nrf1 regulates proteotoxic stress-induced autophagy

inferred← citeshttps://doi.org/10.1101/2023.12.19.572332openalex-snapshot

Reconstitution of autophagosomal membrane tethering reveals that Atg11 can bind and cluster vesicles on cargo mimetics

inferred← citeshttps://doi.org/10.1101/2024.08.06.606738openalex-snapshot

Autophagosomes coordinate an AKAP11-dependent regulatory checkpoint that shapes neuronal PKA signaling

inferred← citeshttps://doi.org/10.1101/2024.09.09.611943openalex-snapshot

Presynapses are mitophagy pit stops that prevent axon degeneration

inferred← citeshttps://doi.org/10.1101/2025.02.11.637156openalex-snapshot

Pneumolysin-dependent and independent non-canonical autophagy processes mediate host defense against pneumococcal infection

inferred← citeshttps://doi.org/10.1101/2025.03.24.645038openalex-snapshot

ATG2A interacts with RAB1A and ARFGAP1 positive membranes during autophagosome biogenesis

inferred← citeshttps://doi.org/10.1101/2025.08.25.671700openalex-snapshot

A singular lipid composition supports the progression of plant autophagy

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