Review
Nature Reviews Molecular Cell Biology 10, 104-115 (February 2009) | doi:10.1038/nrm2630
Molecular mechanisms of proteasome assembly
Shigeo Murata1, Hideki Yashiroda1 & Keiji Tanaka2 About the authors
Abstract
The 26S proteasome is a highly conserved protein degradation machine that consists of the 20S proteasome and 19S regulatory particles, which include 14 and 19 different polypeptides, respectively. How the proteasome components are assembled is a fundamental question towards understanding the process of protein degradation and its functions in diverse biological processes. Several proteasome-dedicated chaperones are involved in the efficient and correct assembly of the 20S proteasome. These chaperones help the initiation and progression of the assembly process by transiently associating with proteasome precursors. By contrast, little is known about the assembly of the 19S regulatory particles, but several hints have emerged.
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Author affiliations
- Laboratory of Protein Metabolism, Department of Integrated Biology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
- Laboratory of Frontier Science, Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan.
Correspondence to: Keiji Tanaka2 Email: tanaka-kj@igakuken.or.jp
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