| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print June 24, 2003
IGBMC, CNRS/INSERM/ULP, Illkirch 67404
Corresponding Author: cegly{at}igbmc.u-strasbg.fr
In eukaryotic cells, liganded RARg2/RXRa heterodimers activate the transcription of RA-target genes and then are degraded through the ubiquitin-proteasome pathway. In this study we dissected the role of the RARg_ and RXRa partners as well as of their respective AF-1 and AF-2 domains in the processes of transactivation and degradation. RARg2 is the “engine” initiating transcription and its own degradation subsequent to ligand binding. Integrity of its AF2-domain and phosphorylation of its AF-1 domain are required for both the degradation and the transactivation of the receptor. Deletion of the whole AF-1 domain does not impair these processes, but shifts the receptor towards other proteolytic pathways through RXRa. In contrast, RXRa plays only a modulatory role, cooperating with RARg2 through its AF-2 domain and its phosphorylated AF-1 domain, in both the transcription activity and the degradation of the RARg2/RXRa heterodimers. Our results underline that the AF-1 and AF-2 domains of each heterodimer partner cooperate with each other and that this cooperation is relevant for both the transcription and degradation processes.
J. Biol. Chem, 10.1074/jbc.M304952200
Submitted on May 12, 2003
Revised on June 23, 2003
Accepted on June 24, 2003
The AF-1 and AF-2 domains of RAR
2 and RXR 
cooperate for triggering the transactivation and the degradation of RAR 2/RXR heterodimers
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  Z. Vucetic, Z. Zhang, J. Zhao, F. Wang, K. J. Soprano, and D. R. Soprano Acinus-S' Represses Retinoic Acid Receptor (RAR)-Regulated Gene Expression through Interaction with the B Domains of RARs Mol. Cell. Biol., April 15, 2008; 28(8): 2549 - 2558. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Lattuada, P. Vigano, S. Mangioni, J. Sassone, S. Di Francesco, M. Vignali, and A. M. Di Blasio Accumulation of Retinoid X Receptor-{alpha} in Uterine Leiomyomas Is Associated with a Delayed Ligand-Dependent Proteasome-Mediated Degradation and an Alteration of Its Transcriptional Activity Mol. Endocrinol., March 1, 2007; 21(3): 602 - 612. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. A. Bogoyevitch and B. Kobe Uses for JNK: the Many and Varied Substrates of the c-Jun N-Terminal Kinases Microbiol. Mol. Biol. Rev., December 1, 2006; 70(4): 1061 - 1095. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Narayanan, V. A. T. Sepulveda, M. Falzon, and N. L. Weigel The Functional Consequences of Cross-talk between the Vitamin D Receptor and ERK Signaling Pathways Are Cell-specific J. Biol. Chem., November 5, 2004; 279(45): 47298 - 47310. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. D.-C. Arce, U. Soto, J. van Riggelen, E. Schwarz, H. z. Hausen, and F. Rosl Ectopic Expression of Nonliganded Retinoic Acid Receptor {beta} Abrogates AP-1 Activity by Selective Degradation of c-Jun in Cervical Carcinoma Cells J. Biol. Chem., October 29, 2004; 279(44): 45408 - 45416. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
