Reversible phosphorylation of the 26S proteasome.
10.1007/s13238-017-0382-x
- Author:
Xing GUO
1
;
Xiuliang HUANG
2
;
Mark J CHEN
3
Author Information
1. The Life Sciences Institute of Zhejiang University, Hangzhou, 310058, China. xguo@zju.edu.cn.
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.
- Publication Type:Journal Article
- Keywords:
kinase;
phosphatase;
phosphorylation;
proteasome;
protein degradation
- MeSH:
Animals;
Humans;
Phosphoprotein Phosphatases;
genetics;
metabolism;
Phosphorylation;
genetics;
Proteasome Endopeptidase Complex;
genetics;
metabolism;
Protein Kinases;
genetics;
metabolism
- From:
Protein & Cell
2017;8(4):255-272
- CountryChina
- Language:English
-
Abstract:
The 26S proteasome at the center of the ubiquitin-proteasome 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.
