Volume 8 Issue 4
Apr.  2017
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Xing Guo, Xiuliang Huang, Mark J. Chen. Reversible phosphorylation of the 26S proteasome[J]. Protein&Cell, 2017, 8(4): 255-272. doi: 10.1007/s13238-017-0382-x
Citation: Xing Guo, Xiuliang Huang, Mark J. Chen. Reversible phosphorylation of the 26S proteasome[J]. Protein&Cell, 2017, 8(4): 255-272. doi: 10.1007/s13238-017-0382-x

Reversible phosphorylation of the 26S proteasome

doi: 10.1007/s13238-017-0382-x
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This work was supported by the startup funding from Zhejiang University, Fundamental Research Funds for the Central Universities (2016QN81011) and National Natural Science Foundation of China (31671391) to X.G. M.J.C is supported by the Genentech postdoctoral program.

  • Received Date: 2016-12-15
  • Rev Recd Date: 2017-01-26
  • 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.
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