Deep research synthesis of ATG5 function and literature
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ATG5 is a core human autophagy protein that forms the ATG12-ATG5-ATG16L1 E3-like complex for LC3 lipidation
"ATG5 (UniProt Q9H1Y0) is a core human autophagy protein in the ATG5 family, bearing ubiquitin-like folds that enable conjugation with ATG12 and assembly of the ATG12–ATG5–ATG16L1 complex, which functions as an E3-like ligase for LC3/ATG8 lipidation during autophagosome biogenesis"
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The complex localizes to the convex surface of the phagophore and dissociates upon autophagosome completion
"The ATG12–ATG5–ATG16L1 complex preferentially associates with the convex surface of the growing isolation membrane (phagophore) and detaches/recycles once autophagosome closure is achieved"
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Calpain-mediated cleavage of ATG5 produces a pro-apoptotic fragment that translocates to mitochondria
"Calpain-mediated cleavage of ATG5 yields a pro-apoptotic fragment that migrates to mitochondria and promotes apoptosis, highlighting crosstalk between autophagy machinery and cell death programs"
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy.
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Demonstrated that human ATG12 is covalently attached to ATG5 via an isopeptide bond at Lys-130
"Mutagenic analyses suggested that this conjugation was formed via an isopeptide bond between the C-terminal glycine of hApg12 and Lys-130 of hApg5."
The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3.
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Showed hApg7p is an E1-like enzyme essential for the hApg12p conjugation system
"Overexpression of hApg7p enhances the formation of the hApg5p.hApg12p conjugate, indicating that hApg7p is an E1-like enzyme essential for the hApg12p conjugation system."
Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes.
Large-scale mapping of human protein-protein interactions by mass spectrometry.
The Atg5 Atg12 conjugate associates with innate antiviral immune responses.
Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains.
The autophagy machinery is required to initiate hepatitis C virus replication.
The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy.
Network organization of the human autophagy system.
A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens.
A mammalian autophagosome maturation mechanism mediated by TECPR1 and the Atg12-Atg5 conjugate.
Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts.
Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection.
Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy.
Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-dependent and -independent autophagy.
FIP200 regulates targeting of Atg16L1 to the isolation membrane.
Structural basis of ATG3 recognition by the autophagic ubiquitin-like protein ATG12.
Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners.
Mutation in ATG5 reduces autophagy and leads to ataxia with developmental delay.
Hepatitis C virus triggers Golgi fragmentation and autophagy through the immunity-related GTPase M.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
RAB33B recruits the ATG16L1 complex to the phagophore via a noncanonical RAB binding protein.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Multimodal cell maps as a foundation for structural and functional genomics.
LC3 binds the autophagosome membrane Atg5-Atg12 complex
ATG16L1 complex transfers LC3 from ATG3 to PE
WIPI2 binds ATG12:ATG5:ATG16L
ATG10 dissociates from ATG12:ATG5
ATG10 transfers ATG12 from ATG10 to ATG5
LC3 binds the autophagosome membrane Atg5-Atg12 complex