Ubiquitin-like-conjugating enzyme ATG3 (ATG3)

Ubiquitin-like-conjugating enzyme ATG3 (ATG3) is a central E2-like enzyme involved in the autophagy pathway, specifically mediating the lipidation of LC3 (microtubule-associated protein 1 light chain 3, Atg8 in yeast) to phosphatidylethanolamine (PE), a critical step in autophagosome formation[1][2][3][5][7]. ATG3 functions in complex with ATG7 (E1-like enzyme) and the ATG12–ATG5–ATG16L1 complex (E3-like ligase) and facilitates recruitment and elongation of autophagic membranes. Its core role extends to both canonical autophagy and noncanonical LC3 lipidation events, impacting processes including tumorigenesis, infection response, and cell differentiation. While best known for its autophagy-dependent cellular housekeeping, emerging evidence points to autophagy-independent functions in mitosis and cell cycle regulation. Loss of ATG3 results in severe defects in autophagosome formation and is lethal in mammals[1][2][3][7]. There are no approved therapeutic agents that selectively target ATG3, though it has potential as a drug target and disease biomarker in conditions linked to autophagy dysfunction[1][3].

Other names

Autophagy-related protein 3APG3APG3LAPG3-likehApg3PC3-96FLJ22125MGC15201DKFZp564M1178Protein PC3-96

NA (no approved drugs, mechanism of action would be anticipated as inhibition of ATG3 enzymatic/lipidation activity or modulation of autophagy pathway, based on general autophagy-targeted pharmacology, but specific small molecule or antibody mechanisms are not defined in current literature)[1][3].