Structural highlights
Publication Abstract from PubMed
Macroautophagy is a bulk clearance mechanism in which the double-membraned phagophore grows and engulfs cytosolic material. In yeast, the phagophore nucleates from a cluster of 20-30 nm diameter Atg9-containing vesicles located at a multiprotein assembly known as the preautophagosomal structure (PAS). The crystal structure of a 2:2:2 complex of the earliest acting PAS proteins, Atg17, Atg29, and Atg31, was solved at 3.05 A resolution. Atg17 is crescent shaped with a 10 nm radius of curvature. Dimerization of the Atg17-Atg31-Atg29 complex is critical for both PAS formation and autophagy, and each dimer contains two separate and complete crescents. Upon induction of autophagy, Atg17-Atg31-Atg29 assembles with Atg1 and Atg13, which in turn initiates the formation of the phagophore. The C-terminal EAT domain of Atg1 was shown to sense membrane curvature, dimerize, and tether lipid vesicles. These data suggest a structural mechanism for the organization of Atg9 vesicles into the early phagophore.
Architecture of the atg17 complex as a scaffold for autophagosome biogenesis.,Ragusa MJ, Stanley RE, Hurley JH Cell. 2012 Dec 21;151(7):1501-12. doi: 10.1016/j.cell.2012.11.028. Epub 2012 Dec , 6. PMID:23219485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ragusa MJ, Stanley RE, Hurley JH. Architecture of the atg17 complex as a scaffold for autophagosome biogenesis. Cell. 2012 Dec 21;151(7):1501-12. doi: 10.1016/j.cell.2012.11.028. Epub 2012 Dec , 6. PMID:23219485 doi:http://dx.doi.org/10.1016/j.cell.2012.11.028
