NDLI: Site-specific acetylation of the proteasome activator REGÎ³ directs its heptameric structure and functions.

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Site-specific acetylation of the proteasome activator REGÎ³ directs its heptameric structure and functions.

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Site-specific acetylation of the proteasome activator REGÎ³ directs its heptameric structure and functions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wei, Haibin Zhou, Li Wang, Weicang Wang, Chuangui Wang, Ying Ji, Lei Zhang, Pei Shan, Peipei Jung, Sung Yun Wang, Yan Yang, Yuanyuan Zhou, Qingxia Liu, Jiang Liu, Jian Long, Weiwen Li, Xiaotao Li, Lei Zhang, Bianhong
Description	Author Affiliation: Liu J ( Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences, School of Life Sciences, East China Normal University, Shanghai 200241, China.)
Abstract	The proteasome activator REGÎ³ has been reported to promote degradation of steroid receptor coactivator-3 and cyclin-dependent kinase inhibitors p21, p16, and p19 in a ubiquitin- and ATP-independent manner. A recent comparative analysis of REGÎ³ expression in mouse and human tissues reveals a unique pattern of REGÎ³ in specific cell types, suggesting undisclosed functions and biological importance of this molecule. Despite the emerging progress made in REGÎ³-related studies, how REGÎ³ function is regulated remains to be explored. In this study, we report for the first time that REGÎ³ can be acetylated mostly on its lysine 195 (Lys-195) residue by CREB binding protein (CBP), which can be reversed by sirtuin 1 (SIRT1) in mammalian cells. Site-directed mutagenesis abrogated acetylation at Lys-195 and significantly attenuated the capability of REGÎ³ to degrade its target substrates, p21 and hepatitis C virus core protein. Mechanistically, acetylation at Lys-195 is important for the interactions between REGÎ³ monomers and ultimately influences REGÎ³ heptamerization. Biological analysis of cells containing REGÎ³-WT or REGÎ³-K195R mutant indicates an impact of acetylation on REGÎ³-mediated regulation of cell proliferation and cell cycle progression. These findings reveal a previously unknown mechanism in the regulation of REGÎ³ assembly and activity, suggesting a potential venue for the intervention of the ubiquitin-independent REGÎ³ proteasome activity.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	23
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-06-07
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Autoantigens Metabolism Proteasome Endopeptidase Complex Protein Multimerization Physiology Proteolysis Acetylation Amino Acid Substitution Animals Genetics CREB-Binding Protein Cell Cycle HEK293 Cells HeLa Cells Mice Mice, Knockout Mutation, Missense Ubiquitin Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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