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Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8
- Source :
- The Journal of Cell Biology. Sept 20, 2010, Vol. 190 Issue 6, p965, 9 p.
- Publication Year :
- 2010
-
Abstract
- The molecular details of the biogenesis of double-membraned autophagosomes are poorly understood. We identify the Saccharomyces cerevisiae AAA-adenosine triphosphatase Cdc48 and its substrate-recruiting cofactor Shp1/Ubx1 as novel components needed for autophagosome biogenesis. In mammals, the Cdc48 homologue p97/VCP and the Shp1 homologue p47 mediate Golgi reassembly by extracting an unknown mono-ubiquitinated fusion regulator from a complex. We find no requirement of ubiquitination or the proteasome system for autophagosome biogenesis but detect interaction of Shp1 with the ubiquitin-fold autophagy protein Atg8. Atg8 coupled to phosphatidylethanolamine (PE) is crucial for autophagosome elongation and, in vitro, mediates tethering and hemifusion. Interaction with Shp1 requires an FK motif within the N-terminal non--ubiquitin-like Atg8 domain. Based on our data, we speculate that autophagosome formation, in contrast to Golgi reassembly, requires a complex in which Atg8 functionally substitutes ubiquitin. This, for the first time, would give a rationale for use of the ubiquitin-like Atg8 during macroautophagy and would explain why Atg8-PE delipidation is necessary for efficient macroautophagy. doi/ 10.1083/jcb.201002075
- Subjects :
- Biosynthesis -- Research
Ubiquitin -- Research
Biological sciences
Subjects
Details
- Language :
- English
- ISSN :
- 00219525
- Volume :
- 190
- Issue :
- 6
- Database :
- Gale General OneFile
- Journal :
- The Journal of Cell Biology
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.238653125