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Autophagy. 2016 Nov;12(11):2260-2261. Epub 2016 Aug 25.

Atg8 lipidation is coordinated in a PtdIns3P-dependent manner by the PROPPIN Atg21.

Author information

1
a Institute of Cellular Biochemistry, University Medicine Goettingen , Georg-August-University , Göttingen , Germany.

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.

KEYWORDS:

Atg16; Atg21; Atg8 lipidation; PROPPIN; PtdIns3P

PMID:
27560294
PMCID:
PMC5103337
DOI:
10.1080/15548627.2016.1221564
[Indexed for MEDLINE]
Free PMC Article

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