PFN2a, a new partner of RARα in the cytoplasm.

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

https://www.ncbi.nlm.nih.gov/pubmed/29158086

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