Reactome | The activated LC3 protein is transferred to Cys-263 of ATG3 ...

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created	[InstanceEdit:5681983] Jupe, Steve, 2015-03-04
dbId	5681979
displayName	The activated LC3 protein is transferred to Cys-263 of ATG3 ...
literatureReference	[LiteratureReference:5681995] A ubiquitin-like system mediates protein lipidation [LiteratureReference:5682386] Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p [LiteratureReference:5682883] Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins [LiteratureReference:5682890] The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation
modified	[InstanceEdit:5683589] Jupe, Steve, 2015-03-16
schemaClass	Summation
text	The activated LC3 protein is transferred to Cys-263 of ATG3 through a thioester bond (Ichimura et al. 2000, Tanida et al. 2002). Deletion mutagenesis, biochemical data and modeling suggest that recruitment of ATG3 to the ATG7 N-terminal FAP domain results in presentation of the ATG3 active site to the LC3-ATG7 thioester linkage from the opposing monomer in the ATG7 dimer (Tanida et al. 2012, Klionsky & Schulman 2014).

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