Physical and functional interactions between cellular retinoic acid binding protein II and the retinoic acid-dependent nuclear complex.
Fiche publication
Date publication
octobre 1999
Journal
Molecular and cellular biology
Auteurs
Membres identifiés du Cancéropôle Est :
Pr BASTIE Jean-Noël, Pr CHAMBON Pierre, Dr DELVA Laurent, Dr ROCHETTE-EGLY Cécile, Dr DESPOUY Gilles
Tous les auteurs :
Delva L, Bastie JN, Rochette-Egly C, Kraïba R, Balitrand N, Despouy G, Chambon P, Chomienne C
Lien Pubmed
Résumé
Two sorts of proteins bind to, and mediate the developmental and homeostatic effects of, retinoic acid (RA): the RAR and RXR nuclear receptors, which act as ligand-dependent transcriptional regulators, and the cellular RA binding proteins (CRABPI and CRABPII). CRABPs are generally known to be implicated in the synthesis, degradation, and control of steady-state levels of RA, yet previous and recent data have indicated that they could play a role in the control of gene expression. Here we show for the first time that, both in vitro and in vivo, CRABPII is associated with RARalpha and RXRalpha in a ligand-independent manner in mammalian cells (HL-60, NB-4, and MCF-7). In the nucleus, this protein complex binds the RXR-RAR-specific response element of an RA target gene (RARE-DR5). Moreover, in the presence of retinoids that bind both the nuclear receptors and CRABPII, enhancement of transactivation by RXRalpha-RARalpha heterodimers is observed in the presence of CRABPII. Thus, CRABPII appears to be a novel transcriptional regulator involved in RA signaling.
Mots clés
Bone Marrow Cells, Breast Neoplasms, metabolism, HL-60 Cells, Humans, Nuclear Proteins, metabolism, Protein Binding, Receptors, Retinoic Acid, metabolism, Response Elements, Retinoid X Receptors, Signal Transduction, Teratocarcinoma, metabolism, Transcription Factors, metabolism, Transcriptional Activation, Tumor Cells, Cultured
Référence
Mol. Cell. Biol.. 1999 Oct;19(10):7158-67