Chaperone-mediated pathway of proteasome regulatory particle assembly

Jeroen Roelofs, Soyeon Park, Wilhelm Haas, Geng Tian, Fiona E. McAllister, Ying Huo, Byung-Hoon Lee, Fan Zhang, Yigong Shi, Steven P. Gygi and Daniel Finley ()
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Jeroen Roelofs: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Soyeon Park: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Wilhelm Haas: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Geng Tian: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Fiona E. McAllister: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Ying Huo: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Byung-Hoon Lee: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Fan Zhang: Lewis Thomas Laboratory, Princeton University, Princeton, New Jersey 08544, USA
Yigong Shi: Lewis Thomas Laboratory, Princeton University, Princeton, New Jersey 08544, USA
Steven P. Gygi: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Daniel Finley: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA

Nature, 2009, vol. 459, issue 7248, 861-865

Abstract: Proteasome assembly The proteasome is a large proteolytic machine that degrades ubiquitin-tagged proteins. Substrates are recognized and unfolded by the regulatory particle (RP) and translocated into a central proteolytic chamber called the core particle (CP) where degradation takes place. The CP associates with the RP at either one or both ends. The RP can be further subdivided into the base and lid. Two studies from Finley and colleagues elucidate the pathway of RP assembly. They report the identification of three molecular chaperones that assist in the assembly of the RP. Assembly of the base proceeds through a complex consisting of five proteins, called BP1, which functions as an intermediate in the process. These studies show that RP assembly is a highly orchestrated process.

Date: 2009
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DOI: 10.1038/nature08063

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