Homodimerization of RBPMS2 through a new RRM-interaction motif is necessary to control smooth muscle plasticity.
Bottom Line: RBPMS2 contains only one RNA recognition motif (RRM) while this motif is often repeated in tandem or associated with other functional domains in RRM-containing proteins.We also show that this specific motif is conserved among its homologs and paralogs in vertebrates and in its insect and worm orthologs (CPO and MEC-8, respectively) suggesting a conserved molecular mechanism of action.Our study demonstrates that RBPMS2 possesses an RRM domain harboring both RNA-binding and protein-binding properties and that the newly identified RRM-homodimerization motif is crucial for the function of RBPMS2 at the cell and tissue levels.
Affiliation: INSERM U1046, Université Montpellier 1, Université Montpellier 2, 34295 Montpellier, France.Show MeSH
Related in: MedlinePlus
Mentions: In addition, we also found that dimeric RBPMS2 interacts with elongation factor eEF2, whereas monomeric RBPMS2 does not. Altogether, our experiments drive us to propose a model in which dimeric RBPMS2 could recruit specific protein partner(s) such as translational factor eEF2 in order to connect RBPMS2 and NOGGIN mRNA to the translational machinery complex to promote the SMC dedifferentiation process (Figure 6A). On the opposite way, monomeric RBPMS2 subunit is unable to interact with partners such as eEF2 and to allow the accumulation of NOGGIN mRNA (Figure 6B).
Affiliation: INSERM U1046, Université Montpellier 1, Université Montpellier 2, 34295 Montpellier, France.