Journal
AUTOPHAGY
Volume 16, Issue 6, Pages 1007-1020Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2019.1648117
Keywords
Autophagy; intrinsically disordered region; membrane binding; phospholipids; structure
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Funding
- National Institute of General Medical Sciences [GM128663, GM113132, GM053396, GM131919]
- Protein Folding Diseases FastForward Initiative, University of Michigan
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Macroautophagy/autophagy is a conserved catabolic recycling pathway involving the sequestration of cytoplasmic components within double-membrane vesicles termed autophagosomes. The autophagy-related (Atg) protein Atg13 is a key member of the autophagy initiation complex. The Atg13 C terminus is an intrinsically disordered region (IDR) harboring a binding site for the vacuolar membrane protein Vac8. Recent reports suggest Atg13 acts as a hub to assemble the initiation complex, and also participates in membrane recognition. Here we show that the Atg13 C terminus directly binds to lipid membranes via electrostatic interactions between positively charged residues in Atg13 and negatively charged phospholipids as well as a hydrophobic insertion of a Phe residue. We identified 2 sets of residues in the Atg13 IDR that affect its phospholipid-binding properties; these residues overlap with the Vac8-binding domain of Atg13. Our data indicate that Atg13 binding to phospholipids and Vac8 is mutually exclusive, and both are required for efficient autophagy.
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