Mechanistic Studies of Post-translational Modifications on the Proteasome
LU Hui1),2), LI Yan-Chang2)*, HUANG Xue-Shi1)*
1)Institute of Microbial Pharmaceuticals, College of Life and Health Sciences, Northeastern University, Shenyang 110819, China; 2)State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences(Beijing), Beijing Institute of Lifeomics, Beijing 102206, China
Abstract：The proteasome is the main complex for specific protein degradation in eukaryotic cells, which plays a key role in protein quality control and cell homeostasis maintenance. It is found that abnormal content or function of the proteasome can lead to many human serious diseases such as cancer and neurodegenerative disorders, and several targeted drugs have been developed for the regulation of proteasome activity. Therefore, it is of great academic value and clinical significance to strengthen the research on the precise regulation mechanism of proteasome activity. The content, assembly and activity of the proteasome are regulated rigorously by multiple levels. In this paper, we summarize the composition subunits, structural features, transcriptional regulation and assembly mechanism of proteasome, and focus on the mechanistic regulation and biological significance of post-translational modifications such as phosphorylation, ubiquitination and acetylation on proteasome, which might be helpful to reveal the regulation mechanism of proteasome in the near future.
卢慧, 李衍常, 黄学石. 蛋白酶体翻译后修饰功能机制研究[J]. 中国生物化学与分子生物学报, 2021, 37(6): 710-719.
LU Hui, LI Yan-Chang, HUANG Xue-Shi. Mechanistic Studies of Post-translational Modifications on the Proteasome. Chinese Journal of Biochemistry and Molecular Biol, 2021, 37(6): 710-719.
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