JBC Origene Your Gene Company

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


     


Originally published In Press as doi:10.1074/jbc.M205816200 on July 16, 2002

J. Biol. Chem., Vol. 277, Issue 38, 35088-35096, September 20, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/38/35088    most recent
M205816200v1
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 Sacchetti, P.
Right arrow Articles by Lefebvre, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sacchetti, P.
Right arrow Articles by Lefebvre, P.
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?

Requirements for Heterodimerization between the Orphan Nuclear Receptor Nurr1 and Retinoid X Receptors*

Paola SacchettiDagger , Hélène Dwornik, Pierre Formstecher, Christophe Rachez, and Philippe Lefebvre§

From the INSERM Unité 459, Faculté de Medecine Henri Warembourg, 1 Place de Verdun, Lille 59045, France

The nuclear receptor nurr1 is a transcription factor involved in the development and maintenance of neurons synthesizing the neurotransmitter dopamine. Although the lack of nurr1 expression has dramatic consequences for these cells either in terms of differentiation or survival, the mechanisms by which nurr1 controls gene transcription still remain unclear. In the intent to understand better the modalities of action of this nuclear receptor, we have undertaken a systematic analysis of the transcriptional effects and DNA binding properties of nurr1 as a monomer or when forming dimers with the different isotypes of the retinoic X receptor (RXR). Here, we show that nurr1 acts as a gene activator independently of RXR and through an AF2-independent mechanism. In addition, heterodimerization with RXR is isotype-specific, involves multiple domains in the C-terminal region of nurr1, and requires RXR binding to DNA. RXRalpha -nurr1 and RXRgamma -nurr1 heterodimers bind direct repeat response elements and display no specific requirements with respect to half-site spacing. However, the retinoid responsiveness of DNA-bound heterodimers requires the reiteration of at least three nurr1 binding sites, thereby limiting retinoid-induced nurr1 transcriptional activity to specific direct response elements.


* This work was supported in part by a Marie Curie Fellowship of the European Community Program "Improving Human Research Potential and the Socio-economic Knowledge Base" under Contract HPMF-CT-2001-01362 (to P. S.) and by the INSERM and Association France-Parkinson.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 Recipient of an INSERM poste vert.

§ To whom correspondence should be addressed. Tel.: 33-3-2062-6876; Fax: 33-3-2062-6884; E-mail: p.lefebvre@lille.inserm.fr.


Copyright © 2002 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
K. S. Mix, M. G. Attur, H. Al-Mussawir, S. B. Abramson, C. E. Brinckerhoff, and E. P. Murphy
Transcriptional Repression of Matrix Metalloproteinase Gene Expression by the Orphan Nuclear Receptor NURR1 in Cartilage
J. Biol. Chem., March 30, 2007; 282(13): 9492 - 9504.
[Abstract] [Full Text] [PDF]


Home page
Drug Metab. Dispos.Home page
S. S. Auerbach, J. G. DeKeyser, M. A. Stoner, and C. J. Omiecinski
CAR2 Displays Unique Ligand Binding and RXR{alpha} Heterodimerization Characteristics
Drug Metab. Dispos., March 1, 2007; 35(3): 428 - 439.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
P. Sacchetti, R. Carpentier, P. Segard, C. Olive-Cren, and P. Lefebvre
Multiple signaling pathways regulate the transcriptional activity of the orphan nuclear receptor NURR1
Nucleic Acids Res., November 14, 2006; 34(19): 5515 - 5527.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
F. Q. Pirih, A. Tang, I. C. Ozkurt, J. M. Nervina, and S. Tetradis
Nuclear Orphan Receptor Nurr1 Directly Transactivates the Osteocalcin Gene in Osteoblasts
J. Biol. Chem., December 17, 2004; 279(51): 53167 - 53174.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
X. Cao, W. Liu, F. Lin, H. Li, S. K. Kolluri, B. Lin, Y.-h. Han, M. I. Dawson, and X.-k. Zhang
Retinoid X Receptor Regulates Nur77/Thyroid Hormone Receptor 3-Dependent Apoptosis by Modulating Its Nuclear Export and Mitochondrial Targeting
Mol. Cell. Biol., November 15, 2004; 24(22): 9705 - 9725.
[Abstract] [Full Text] [PDF]


Home page
Mol. Endocrinol.Home page
P. I. Sadate-Ngatchou, D. J. Pouchnik, and M. D. Griswold
Follicle-Stimulating Hormone Induced Changes in Gene Expression of Murine Testis
Mol. Endocrinol., November 1, 2004; 18(11): 2805 - 2816.
[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 © 2002 by the American Society for Biochemistry and Molecular Biology.