JBC Advanced Peptides, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M010185200 on March 5, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16107-16112, May 11, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/19/16107    most recent
M010185200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 Wei, L.-N.
Right arrow Articles by Hu, X.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wei, L.-N.
Right arrow Articles by Hu, X.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Ligand-dependent Formation of Retinoid Receptors, Receptor-interacting Protein 140 (RIP140), and Histone Deacetylase Complex Is Mediated by a Novel Receptor-interacting Motif of RIP140*

Li-Na WeiDagger , Maria Farooqui, and Xinli Hu

From the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455

Receptor-interacting protein 140 (RIP140) interacts with retinoic acid receptor and retinoid X receptor in a ligand-dependent manner and suppresses retinoic acid (RA) induction of its target genes. The receptor-interacting motif is mapped to a C-terminal peptide sequence (LTKTNPILYYMLQK) of RIP140. The functional role of this motif in mediating the suppressive effects of RIP140 on RA induction is demonstrated in mutation studies. RA induces coimmunoprecipitation of histone deacetylase 3 with retinoic acid receptor/retinoid X receptor in the presence of wild type RIP140, but not in the presence of the C-terminal motif-deleted RIP140. A decrease in histone acetylation on the promoter region that carries a RA response element is associated with the expression of wild type RIP140, but not with expression of the mutant RIP140, in a dose-dependent manner. These data provide a molecular explanation for RIP140 acting as a novel ligand-dependent, negative modulator of RA-regulated gene expression.

* This work was supported by National Institutes of Health Grant DK54733, American Cancer Society Grant RPG-99-237-010CNE, and United States Department of Agriculture Grant 98-35200-6264 (to L.-N. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Pharmacology, University of Minnesota, 6-120 Jackson Hall, 321 Church St. SE, Minneapolis, MN 55455-0217. Tel.: 612-625-9402; Fax: 612-625-8408; E-mail: weixx009@tc.umn.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
E. B. Dammer and M. B. Sewer
Phosphorylation of CtBP1 by cAMP-dependent Protein Kinase Modulates Induction of CYP17 by Stimulating Partnering of CtBP1 and 2
J. Biol. Chem., March 14, 2008; 283(11): 6925 - 6934.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. Gupta, S. W. Park, M. Farooqui, and L.-N. Wei
Orphan nuclear receptor TR2, a mediator of preadipocyte proliferation, is differentially regulated by RA through exchange of coactivator PCAF with corepressor RIP140 on a platform molecule GRIP1
Nucleic Acids Res., April 1, 2007; 35(7): 2269 - 2282.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
X. Wei, H. Xu, and D. Kufe
Human Mucin 1 Oncoprotein Represses Transcription of the p53 Tumor Suppressor Gene
Cancer Res., February 15, 2007; 67(4): 1853 - 1858.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
H. Leong, J. R. Sloan, P. D. Nash, and G. L. Greene
Recruitment of Histone Deacetylase 4 to the N-Terminal Region of Estrogen Receptor {alpha}
Mol. Endocrinol., December 1, 2005; 19(12): 2930 - 2942.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
P. Gupta, M. D. M. Huq, S. A. Khan, N.-P. Tsai, and L.-N. Wei
Regulation of Co-repressive Activity of and HDAC Recruitment to RIP140 by Site-specific Phosphorylation
Mol. Cell. Proteomics, November 1, 2005; 4(11): 1776 - 1784.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
M. D. M. Huq and L.-N. Wei
Post-translational Modification of Nuclear Co-repressor Receptor-interacting Protein 140 by Acetylation
Mol. Cell. Proteomics, July 1, 2005; 4(7): 975 - 983.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Kurtev, R. Margueron, K. Kroboth, E. Ogris, V. Cavailles, and C. Seiser
Transcriptional Regulation by the Repressor of Estrogen Receptor Activity via Recruitment of Histone Deacetylases
J. Biol. Chem., June 4, 2004; 279(23): 24834 - 24843.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
S. Sanyal, J. Matthews, D. Bouton, H.-J. Kim, H.-S. Choi, E. Treuter, and J.-A. Gustafsson
Deoxyribonucleic Acid Response Element-Dependent Regulation of Transcription by Orphan Nuclear Receptor Estrogen Receptor-Related Receptor {gamma}
Mol. Endocrinol., February 1, 2004; 18(2): 312 - 325.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
X. Hu, Y. Chen, M. Farooqui, M. C. Thomas, C.-M. Chiang, and L.-N. Wei
Suppressive Effect of Receptor-interacting Protein 140 on Coregulator Binding to Retinoic Acid Receptor Complexes, Histone-modifying Enzyme Activity, and Gene Activation
J. Biol. Chem., January 2, 2004; 279(1): 319 - 325.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
H. Tazawa, W. Osman, Y. Shoji, E. Treuter, J.-A. Gustafsson, and J. Zilliacus
Regulation of Subnuclear Localization Is Associated with a Mechanism for Nuclear Receptor Corepression by RIP140
Mol. Cell. Biol., June 15, 2003; 23(12): 4187 - 4198.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
C. Teyssier, K. Belguise, F. Galtier, V. Cavailles, and D. Chalbos
Receptor-Interacting Protein 140 Binds c-Jun and Inhibits Estradiol-Induced Activator Protein-1 Activity by Reversing Glucocorticoid Receptor-Interacting Protein 1 Effect
Mol. Endocrinol., February 1, 2003; 17(2): 287 - 299.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
Y. Chen, A. Kerimo, S. Khan, and L.-N. Wei
Real-Time Analysis of Molecular Interaction of Retinoid Receptors and Receptor-Interacting Protein 140 (RIP140)
Mol. Endocrinol., November 1, 2002; 16(11): 2528 - 2537.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
N. Vo, C. Fjeld, and R. H. Goodman
Acetylation of Nuclear Hormone Receptor-Interacting Protein RIP140 Regulates Binding of the Transcriptional Corepressor CtBP
Mol. Cell. Biol., September 15, 2001; 21(18): 6181 - 6188.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.