Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140

Christian, Mark and Tullet, Jennifer M A and Parker, Malcolm G (2004) Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140. The Journal of biological chemistry, 279 (15). pp. 15645-15651. ISSN 0021-9258. E-ISSN 1083-351X. (doi:https://doi.org/10.1074/jbc.M313906200) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1074/jbc.M313906200

Abstract

Receptor interacting protein (RIP) 140 is a corepressor that can be recruited to nuclear receptors by means of LXXLL motifs. We have characterized four distinct autonomous repression domains in RIP140, termed RD1-4, that are highly conserved in mammals and birds. RD1 at the N terminus represses transcription in the presence of trichostatin A, suggesting that it functions by a histone deacetylase (HDAC)-independent mechanism. The repressive activity of RD2 is dependent upon carboxyl-terminal binding protein recruitment to two specific binding sites. Use of specific inhibitors indicates that RD2, RD3, and RD4 are capable of functioning by HDAC-dependent and HDAC-independent mechanisms, depending upon cell type.

Item Type: Article
Subjects: Q Science > Q Science (General)
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Jennifer Tullet
Date Deposited: 13 Oct 2014 08:15 UTC
Last Modified: 09 Jul 2015 10:55 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/43247 (The current URI for this page, for reference purposes)
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