Reversible phosphorylation of the 26S proteasome

doi:10.1007/s13238-017-0382-x

Protein Cell

2017, Vol. 8

Issue (4) : 255-272 https://doi.org/10.1007/s13238-017-0382-x

REVIEW

Reversible phosphorylation of the 26S proteasome

Xing Guo¹(

), Xiuliang Huang², Mark J. Chen³

¹. The Life Sciences Institute of Zhejiang University, Hangzhou 310058, China
². Ministry of Education Key Laboratory of Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China
³. Department of Bioinformatics and Computational Biology, Genentech Inc., South San Francisco, CA 94080, USA

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Abstract

The 26S proteasome at the center of the ubiquitinproteasome system (UPS) is essential for virtually all cellular processes of eukaryotes. A common misconception about the proteasome is that, once made, it remains as a static and uniform complex with spontaneous and constitutive activity for protein degradation. Recent discoveries have provided compelling evidence to support the exact opposite insomuch as the 26S proteasome undergoes dynamic and reversible phosphorylation under a variety of physiopathological conditions. In this review, we summarize the history and current understanding of proteasome phosphorylation, and advocate the idea of targeting proteasome kinases/phosphatases as a new strategy for clinical interventions of several human diseases.

Keywords proteasome phosphorylation kinase phosphatase protein degradation

Corresponding Author(s): Xing Guo

Issue Date: 19 May 2017

Cite this article:

Xing Guo,Xiuliang Huang,Mark J. Chen. Reversible phosphorylation of the 26S proteasome[J]. Protein Cell, 2017, 8(4): 255-272.

URL:

https://academic.hep.com.cn/pac/EN/10.1007/s13238-017-0382-x
https://academic.hep.com.cn/pac/EN/Y2017/V8/I4/255

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