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Chaperone-mediated pathway of proteasome regulatory particle assembly

Author

Listed:
  • 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)

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.

Suggested Citation

  • Jeroen Roelofs & Soyeon Park & Wilhelm Haas & Geng Tian & Fiona E. McAllister & Ying Huo & Byung-Hoon Lee & Fan Zhang & Yigong Shi & Steven P. Gygi & Daniel Finley, 2009. "Chaperone-mediated pathway of proteasome regulatory particle assembly," Nature, Nature, vol. 459(7248), pages 861-865, June.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7248:d:10.1038_nature08063
    DOI: 10.1038/nature08063
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    Cited by:

    1. Lei Pang & Yuanzhi Huang & Yilin He & Dong Jiang & Ruixi Li, 2025. "The adaptor protein AP-3β disassembles heat-induced stress granules via 19S regulatory particle in Arabidopsis," Nature Communications, Nature, vol. 16(1), pages 1-20, December.

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