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Updated: Feb 18, 2026

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
Published on: March 5, 2019
PFN2a, a new partner of RARα in the cytoplasm
Dina Andriamoratsiresy1, Aleksandr Piskunov2, Regis Lutzing1
1IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire), INSERM, U596, CNRS, UMR7104, Université de Strasbourg, 1 Rue Laurent Fries, BP 10142, 67404 Illkirch Cedex, France.
Abstract:
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.
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