Work

Structural characterization of theSaccharomyces cerevisiaeautophagy regulatory complex Atg17-Atg31-Atg29

Year: 2013
Type: article
Abstract: Atg17, in complex with Atg29 and Atg31, constitutes a key module of the Atg1 kinase signaling complex and functions as an important organizer of the phagophore assembly site in the yeast Saccharomyces cerevisiae. We have determined the three-dimensional reconstruction of the full S. cerevisiae Atg17-Atg31-Atg29 complex by single-particle electron microscopy. Our structure shows that Atg17-Atg31-Atg29 is dimeric and adopts a relatively rigid and extended "S-shape" architecture with an end-to-end distance of approximately 345 Å. Subunit mapping analysis indicated that Atg17 mediates dimerization and generates a central rod-like scaffold, while Atg31 and Atg29 form two globular domains that are tethered to the concave sides of the scaffold at the terminal regions. Finally, our observation that Atg17 adopts multiple conformations in the absence of Atg31 and Atg29 suggests that the two smaller components play key roles in defining and maintaining the distinct curvature of the ternary complex.
Source: Autophagy
Language: English
Subfield: Cell Biology
Open Access status: bronze
OpenAlex ID: W1990868872
FWCI: 2.06
Cites: 28
Cited by: 40
Related to: 10