LC3:ATG7 dimer binds ATG3

Stable Identifier
R-HSA-5682896
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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The ATG7 dimer with bound LC3 binds ATG3. 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). The activated LC3 protein is transferred to the E2-like enzyme ATG3 through a thioester bond (Ichimura et al. 2000).

Literature References
PubMed ID Title Journal Year
22170151 The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation

Tanida, I, Yamasaki, M, Komatsu, M, Ueno, T

Autophagy 2012
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