Reactome | ATG3 transfers LC3 from ATG7 to ATG3

ATG3 transfers LC3 from ATG7 to ATG3

Stable Identifier

R-HSA-5681981

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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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