PFN2a, a new partner of RARα in the cytoplasm.
Fiche publication
Date publication
janvier 2018
Journal
Biochemical and biophysical research communications
Auteurs
Membres identifiés du Cancéropôle Est :
Dr ROCHETTE-EGLY Cécile
Tous les auteurs :
Andriamoratsiresy D, Piskunov A, Lutzing R, Rochette-Egly C
Lien Pubmed
Résumé
Retinoic acid receptors (RARs) are classically considered as nuclear ligand-dependent regulators of transcription. Here we highlighted a novel face of the RARα subtype: RARα is present in low amounts in the cytoplasm of mouse embryonic fibroblasts (MEFs) where it interacts with profilin2a (PFN2A), a small actin-binding protein involved in filaments polymerization. The interaction involves the N-terminal proline-rich motif (PRM) of RARα and the SH3-like domain of PFN2a. When increased in the cytoplasm, RARα competes with other PFN2a-binding proteins bearing PRMs and involved in actin filaments elongation. Consequently, the actin filament network is altered and MEFs adhesion is decreased. This novel role opens novel avenues for the understanding of pathologies characterized by increased levels of cytoplasmic RARα.
Mots clés
Actin Cytoskeleton, metabolism, Animals, Cells, Cultured, Cytoplasm, metabolism, Fibroblasts, metabolism, Mice, Profilins, metabolism, Protein Binding, Protein Interaction Mapping, Retinoic Acid Receptor alpha, metabolism
Référence
Biochem. Biophys. Res. Commun.. 2018 01 1;495(1):846-853