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J. Biol. Chem., Vol. 278, Issue 8, 6355-6362, February 21, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/8/6355    most recent M210697200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Despouy, G. Articles by Delva, L. Search for Related Content PubMed PubMed Citation Articles by Despouy, G. Articles by Delva, L. Social Bookmarking                      What's this?

Cyclin D3 Is a Cofactor of Retinoic Acid Receptors, Modulating Their Activity in the Presence of Cellular Retinoic Acid-binding Protein II^*

Gilles Despouy^§, Jean-Noël Bastie, Sylvie Deshaies, Nicole Balitrand, Alexandra Mazharian, Cécile Rochette-Egly^¶, Christine Chomienne, and Laurent Delva

From the  Laboratoire de Biologie Cellulaire Hématopoïétique, Equipe Mixte Inserm 00-03, Institut Universitaire d'Hématologie, Hôpital Saint-Louis, 1 Avenue Claude Vellefaux, Paris 75010 and the ^¶ Institut de Génétique et de Biologie Moléculaire et Cellulaire, Unité Mixte de Recherches 7104, 67404 Illkirch, Cedex France

Ligand-induced transcription activation of retinoic acid (RA) target genes by nuclear receptors (retinoic acid (RAR) and retinoid X (RXR) receptors) depends on the recruitment of coactivators. We have previously demonstrated that the small 15-kDa cellular RA-binding protein II (CRABPII) is a coactivator present in the RA-dependent nuclear complex. As identifying cell-specific partners of CRABPII might help to understand the novel control of RA signaling, we performed a yeast two-hybrid screen of a hematopoietic HL-60 cDNA library using human CRABPII as bait and have subsequently identified human cyclin D3 as a partner of CRABPII. Cyclin D3 interacted with CRABPII in a ligand-independent manner and equally bound RAR, but not RXR, and only in the presence of RA. We further show that cyclin D3 positively modulated RA-mediated transcription through CRABPII. Therefore, cyclin D3 may be part of a ternary complex with CRABPII and RAR. Finally, we show that cyclin D3 expression paralleled HL-60 differentiation and arrest of cell growth. These findings led us to speculate that control of cell proliferation during induction of differentiation may directly involve, at the transcriptional level, nuclear receptors, coactivators, and proteins of the cell cycle in a cell- and nuclear receptor-specific manner.

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