spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Summary Freely available
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Related articles in JCS
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jepsen, K.
Right arrow Articles by Rosenfeld, M. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jepsen, K.
Right arrow Articles by Rosenfeld, M. G.

Biological roles and mechanistic actions of co-repressor complexes

Kristen Jepsen1 and Michael G. Rosenfeld1,*

1 Howard Hughes Medical Institute, Department and School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 920393-0648, USA



View larger version (29K):

[in a new window]
 
Fig. 1. (A) Transcriptional repression by nuclear receptors is regulated by recruitment of the co-repressors N-CoR and/or SMRT. (B) The domains of N-CoR/SMRT. Repression domains (RI, RII, RIII) and SANT domains (A and B) are indicated, as are interaction domains for HDACs, nuclear receptors (I and II) and other transcription factors. (C) N-CoR—SMRT compexes. Biochemical purification techniques have revealed several different complexes recruited by N-CoR and/or SMRT (Jones et al., 2001Go; Li et al., 2000Go; Underhill et al., 2000Go; Wen et al., 2000Go; Guenther et al., 2000Go).

 


View larger version (29K):

[in a new window]
 
Fig. 2. Other HDAC-containing co-repressor complexes identified by biochemical purification, including the Sin 3-SAP (Sin-associated proteins) complex (Zhang et al., 1997Go; Zhang et al., 1998cGo), the NURD (nucleosome remodeling and histone deacetylation) complex (Tong et al., 1998Go; Xue et al., 1998Go; Zhang et al., 1998bGo; Zhang et al., 1999Go), a NURD-related HDAC-complex (Humphrey et al., 2001Go) and a CoREST-HDAC complex (Humphrey et al., 2001Go; You et al., 2001Go). Dashed outlines indicate the molecule that was used to purify each complex.

 





© The Company of Biologists Ltd 2002