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A conserved ATG2-GABARAP interaction is critical for phagophore closure

https://doi.org/10.1101/624627
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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.201338003openalex-snapshot
Structural determinants in GABARAP required for the selective binding and recruitment of ALFY to LC3B‐positive structures
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.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.febslet.2010.01.018openalex-snapshot
Atg8‐family interacting motif crucial for selective autophagy
inferredcites →https://doi.org/10.1016/j.jmb.2011.05.003openalex-snapshot
Characterization of the Interaction of GABARAPL-1 with the LIR Motif of NBR1
inferredcites →https://doi.org/10.1016/j.molcel.2009.01.020openalex-snapshot
A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates
inferredcites →https://doi.org/10.1016/j.molcel.2013.12.014openalex-snapshot
Interactions between Autophagy Receptors and Ubiquitin-like Proteins Form the Molecular Basis for Selective Autophagy
inferredcites →https://doi.org/10.1016/j.molcel.2014.11.006openalex-snapshot
PLEKHM1 Regulates Autophagosome-Lysosome Fusion through HOPS Complex and LC3/GABARAP Proteins
inferredcites →https://doi.org/10.1016/j.molcel.2015.11.019openalex-snapshot
Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy
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/embor.2009.256openalex-snapshot
Nix is a selective autophagy receptor for mitochondrial clearance
inferredcites →https://doi.org/10.1038/nature09204openalex-snapshot
Network organization of the human autophagy system
inferredcites →https://doi.org/10.1038/ncb1846openalex-snapshot
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
inferredcites →https://doi.org/10.1038/ncb1854openalex-snapshot
Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1–phosphatidylinositol-3-kinase complex
inferredcites →https://doi.org/10.1038/ncb2979openalex-snapshot
Cargo recognition and trafficking in selective autophagy
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/nmeth.2019openalex-snapshot
Fiji: an open-source platform for biological-image analysis
inferredcites →https://doi.org/10.1038/nprot.2013.143openalex-snapshot
Genome engineering using the CRISPR-Cas9 system
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/s41594-019-0203-4openalex-snapshot
Atg2 mediates direct lipid transfer between membranes for autophagosome formation
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/10.1073/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/10.1074/jbc.c700195200openalex-snapshot
The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy
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.m115.686915openalex-snapshot
FYCO1 Contains a C-terminally Extended, LC3A/B-preferring LC3-interacting Region (LIR) Motif Required for Efficient Maturation of Autophagosomes during Basal Autophagy
inferredcites →https://doi.org/10.1074/jbc.m702824200openalex-snapshot
p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy
inferredcites →https://doi.org/10.1074/jbc.m803180200openalex-snapshot
The Atg18-Atg2 Complex Is Recruited to Autophagic Membranes via Phosphatidylinositol 3-Phosphate and Exerts an Essential Function
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/10.1080/15548627.2015.1100356openalex-snapshot
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
inferredcites →https://doi.org/10.1080/15548627.2015.1111503openalex-snapshot
Analysis of the native conformation of the LIR/AIM motif in the Atg8/LC3/GABARAP-binding proteins
inferredcites →https://doi.org/10.1080/15548627.2017.1356978openalex-snapshot
iLIR@viral: A web resource for LIR motif-containing proteins in viruses
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/10.1080/15548627.2019.1581009openalex-snapshot
Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs
inferredcites →https://doi.org/10.1080/15548627.2019.1590519openalex-snapshot
Targeted interplay between bacterial pathogens and host autophagy
inferredcites →https://doi.org/10.1080/15548627.2019.1606636openalex-snapshot
Human LC3 and GABARAP subfamily members achieve functional specificity via specific structural modulations
inferredcites →https://doi.org/10.1083/jcb.201603039openalex-snapshot
mito-QC illuminates mitophagy and mitochondrial architecture in vivo
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.201807019openalex-snapshot
VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites
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/10.1091/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.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/10.1111/tra.12640openalex-snapshot
TRAPPC11 functions in autophagy by recruiting ATG2B‐WIPI4/WDR45 to preautophagosomal membranes
inferredcites →https://doi.org/10.1126/science.1205405openalex-snapshot
Phosphorylation of the Autophagy Receptor Optineurin Restricts Salmonella Growth
inferredcites →https://doi.org/10.1242/jcs.156034openalex-snapshot
Ultrastructural analysis of autophagosome organization using mammalian autophagy-deficient cells
inferredcites →https://doi.org/10.1371/journal.pgen.1007020openalex-snapshot
A Rab5 GTPase module is important for autophagosome closure
inferredcites →https://doi.org/10.15252/embj.201796697openalex-snapshot
Molecular definitions of autophagy and related processes
inferredcites →https://doi.org/10.15252/embr.201643587openalex-snapshot
Structural and functional analysis of the GABARAP interaction motif (GIM)
inferredcites →https://doi.org/10.18388/abp.2011_2248openalex-snapshot
Human hAtg2A protein expressed in yeast is recruited to preautophagosomal structure but does not complement autophagy defects of atg2Δ strain.
inferredcites →https://doi.org/10.4161/auto.19496openalex-snapshot
Guidelines for the use and interpretation of assays for monitoring autophagy
inferredcites →https://doi.org/10.4161/auto.28260openalex-snapshot
iLIR
inferredcites →https://doi.org/10.4161/auto.4451openalex-snapshot
Dissection of the Autophagosome Maturation Process by a Novel Reporter Protein, Tandem Fluorescent-Tagged LC3
inferredcites →https://doi.org/10.4161/auto.6.4.11863openalex-snapshot
Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation
inferredcites →https://doi.org/10.4161/auto.7.3.14487openalex-snapshot
Selective autophagy mediated by autophagic adapter proteins

What points at this work

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

inferred← citeshttps://doi.org/10.1016/j.ceb.2019.12.001openalex-snapshot
The ATG conjugation systems in autophagy
inferred← citeshttps://doi.org/10.1016/j.jmb.2019.07.016openalex-snapshot
Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors
inferred← citeshttps://doi.org/10.1016/j.molcel.2021.10.024openalex-snapshot
Multilayered regulation of autophagy by the Atg1 kinase orchestrates spatial and temporal control of autophagosome formation
inferred← citeshttps://doi.org/10.3389/fpls.2020.00565openalex-snapshot
Recent Advances in Membrane Shaping for Plant Autophagosome Biogenesis
inferred← citeshttps://doi.org/10.3390/cells8090973openalex-snapshot
Mechanisms and Pathophysiological Roles of the ATG8 Conjugation Machinery
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