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Mol Cell Proteomics. 2010 Aug;9(8):1666-77. doi: 10.1074/mcp.R000002-MCP201. Epub 2010 May 13.

Toward an integrated structural model of the 26S proteasome.

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  • 1Department of Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany. foerster@biochem.mpg.de

Abstract

The 26S proteasome is the end point of the ubiquitin-proteasome pathway and degrades ubiquitylated substrates. It is composed of the 20S core particle (CP), where degradation occurs, and the 19S regulatory particle (RP), which ensures substrate specificity of degradation. Whereas the CP is resolved to atomic resolution, the architecture of the RP is largely unknown. We provide a comprehensive analysis of the current structural knowledge on the RP, including structures of the RP subunits, physical protein-protein interactions, and cryoelectron microscopy data. These data allowed us to compute an atomic model for the CP-AAA-ATPase subcomplex. In addition to this atomic model, further subunits can be mapped approximately, which lets us hypothesize on the substrate path during its degradation.

PMID:
20467039
[PubMed - indexed for MEDLINE]
PMCID:
PMC2938054
Free PMC Article
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