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Nucleic Acids Research 2005 33(13):4311-4321; doi:10.1093/nar/gki745
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Published online 29 July 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

The proliferating cell nuclear antigen regulates retinoic acid receptor transcriptional activity through direct protein–protein interaction

Perrine J. Martin, Virginie Lardeux and Philippe Lefebvre*

INSERM U459 and Ligue Nationale contre le Cancer, Faculté de Médecine de Lille 1 place de Verdun 59045 Lille cedex, France

*To whom correspondence should be addressed. Tel: +33 3 20626876; Fax: +33 3 20 626884; Email: p.lefebvre{at}lille.inserm.fr

Received May 4, 2005. Revised June 16, 2005. Accepted July 13, 2005.

Retinoic acid receptors (RARs) interact, in a ligand-dependent fashion, with many coregulators that participate in a wide spectrum of biological responses, ranging from embryonic development to cellular growth control. The transactivating function of these ligand-inducible transcription factors reside mainly, but not exclusively, in their ligand-binding domain (AF2), which recruits or dismiss coregulators in a ligand-dependent fashion. However, little is known about AF2-independent function(s) of RARs. We have isolated the proliferating cell nuclear antigen (PCNA) as a repressor of RAR transcriptional activity, able to interact with an AF2-crippled RAR. The N-terminus of PCNA interacts directly with the DNA-binding domain of RAR, and PCNA is recruited to a retinoid-regulated promoter in intact cells. This interaction affects the transcriptional response to retinoic acid in a promoter-specific manner, conferring an unanticipated role to PCNA in transcriptional regulation. Our findings also suggest a role for RAR as a factor coordinating DNA transcription and repair.


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