National Changhua University of Education Institutional Repository : Item 987654321/1833
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 6507/11669
Visitors : 29719651      Online Users : 404
RC Version 3.2 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search
LoginUploadHelpAboutAdminister

Please use this identifier to cite or link to this item: http://ir.ncue.edu.tw/ir/handle/987654321/1833

Title: Histone Deacetylase 3 (HDAC3) Activity is Regulated by Interaction with Protein Serine/Threonine Phosphatase 4
Authors: Zhang X;Ozawa Y;Lee H;Wen YD;Tan TH;Wadzinski BE;Seto E
Contributors: 生物學系
Keywords: HDAC3
histone deacetylation
protein phosphatase
PP4
Date: 2005
Issue Date: 2010-11-15T06:59:57Z
Abstract: Histone deacetylase 3 (HDAC3) is one of four members of the human class I HDACs that regulates gene expression by deacetylation of histones and nonhistone proteins. Early studies have suggested that HDAC3 activity is regulated by association with the corepressors N-CoR and SMRT. Here we demonstrate that, in addition to protein–protein interactions with NCoR/SMRT, the activity of HDAC3 is regulated by both phosphorylation and dephosphorylation. A protein kinase CK2 phosphoacceptor site in the HDAC3 protein was identified at position Ser424, which is a nonconserved residue among the class I HDACs. Mutation of this residue was found to reduce deacetylase activity. Interestingly, unlike other class I HDACs, HDAC3 uniquely copurifies with the catalytic and regulatory subunits of the protein serine/threonine phosphatase 4 complex (PP4c/PP4R1). Furthermore, HDAC3 complexes displayed protein phosphatase activity and a series of subsequent mutational analyses revealed that the N terminus of HDAC3 (residues 1–122) was both necessary and sufficient for HDAC3–PP4c interactions. Significantly, both overexpression and siRNA knock-down approaches, and analysis of cells devoid of PP4c, unequivocally show that HDAC3 activity is inversely proportional to the cellular abundance of PP4c. These findings therefore further highlight the importance of protein–protein interactions and extend the significance of dephosphorylation in the regulation of HDAC activity, as well as present a novel alternative pathway by which HDAC3 activity is regulated.
Relation: Genes & Development. 19(7):827-839. (SCI)
Appears in Collections:[Department of Biology] Periodical Articles

Files in This Item:

There are no files associated with this item.



All items in NCUEIR are protected by copyright, with all rights reserved.

 


DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback