title: Atg8 lipidation is coordinated in a PtdIns3P-dependent manner by the PROPPIN Atg21.
abstract: In Saccharomyces cerevisiae Atg8 coupled to phosphatidylethanolamine is a key component of autophagosome biogenesis. Atg21 binds via 2 sites at the circumference of its β-propeller to PtdIns3P at the phagophore assembly site (PAS). It recruits and arranges both Atg8 and Atg16, which is part of the E3-like ligase complex Atg12-Atg5-Atg16. Binding of Atg8 to Atg21 requires the FK-motif within the N-terminal-helical domain of Atg8 and D146 at the top of the Atg21 β-propeller. Atg16 binds via D101 and E102 within its coiled-coil domain to Atg21.
authors: a Institute of Cellular Biochemistry, University Medicine Goettingen , Georg-August-University , Göttingen , Germany.
authors: Roswitha
authors: R
authors: Krick
authors: a Institute of Cellular Biochemistry, University Medicine Goettingen , Georg-August-University , Göttingen , Germany.
authors: Michael
authors: M
authors: Thumm
mesh_terms: D008055:Lipids / Q000737:chemistry*; D008954:Models, Biological; D010588:Phagosomes / Q000378:metabolism; D018129:Phosphatidylinositol Phosphates / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D008055:Lipids; D018129:Phosphatidylinositol Phosphates; D029701:Saccharomyces cerevisiae Proteins; C055525:phosphatidylinositol 3-phosphate
keywords: Atg16; Atg21; Atg8 lipidation; PROPPIN; PtdIns3P