ATG3 transfers LC3 from ATG7 to ATG3

Stable Identifier
Reaction [transition]
Homo sapiens
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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).
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, Komatsu, M, Yamasaki, M, Ueno, T

Autophagy 2012
11825910 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

Tanida, I, Tanida-Miyake, E, Komatsu, M, Kominami, E, Ueno, T

J. Biol. Chem. 2002
24747438 Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3

Nath, S, Shteyn, V, Yamamoto, A, Melia, TJ, Dancourt, J, Bewersdorf, J, Nag, S, Puente, G, Antonny, B, Fong, WM

Nat. Cell Biol. 2014
Catalyst Activity

Atg8 ligase activity of CysO572-ATG7-LC3:ATG7:ATG3 [cytosol]

Orthologous Events
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