The ATG20 and SNX4/Atg24 proteins have been identified in a screen for mutants defective in a type of selective macroautophagy/autophagy. Both proteins are connected to the ATG1 kinase complex, which is involved in autophagy initiation, and bind phosphatidylinositol-3-phosphate. ATG20 and SNX4 contain putative BAR domains, suggesting a possible role in membrane deformation, but they have been relatively uncharacterized. Here we demonstrate that, in addition to its function in selective autophagy, ATG20 plays a critical role in the efficient induction of nonselective autophagy. ATG20 is a dynamic posttranslationally modified protein that engages both structurally stable (PX and BAR) and intrinsically disordered domains for its function. In addition to its PX and BAR domains, ATG20 uses a third membrane-binding module, a membrane-inducible amphipathic helix present in a previously undescribed location in ATG20 within the putative BAR domain. Taken together, these findings yield insights into the molecular mechanism of the autophagy machinery.

• PMID: 29114050
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Journal Article | Research Support, N.I.H., Extramural | Research Support, N.I.H., Intramural | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, Non-P.H.S.

Authors

Popelka H, Damasio A, Hinshaw JE, Klionsky DJ, Ragusa MJ

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