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Homodimerization of RBPMS2 through a new RRM-interaction motif is necessary to control smooth muscle plasticity.

Sagnol S, Yang Y, Bessin Y, Allemand F, Hapkova I, Notarnicola C, Guichou JF, Faure S, Labesse G, de Santa Barbara P - Nucleic Acids Res. (2014)

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.

View Article: PubMed Central - PubMed

Affiliation: INSERM U1046, Université Montpellier 1, Université Montpellier 2, 34295 Montpellier, France.

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Model of the action of RBPMS2 homodimerization in the SMC dedifferentiation process. Homodimeric RBPMS2 complex interacts with eEF2, an essential member of the eukaryote translational machinery that allows the accumulation of NOGGIN mRNA that will be further translated to inhibit BMP pathway activity (9) and to trigger the dedifferentiation of the SMCs (A). Disruption of RBPMS2 homodimerization through Leu to Glu substitution in position 49 leads to monomeric RBPMS2 proteins unable to interact with eEF2 and inefficient to induce the dedifferentiation process (B).
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Figure 6: Model of the action of RBPMS2 homodimerization in the SMC dedifferentiation process. Homodimeric RBPMS2 complex interacts with eEF2, an essential member of the eukaryote translational machinery that allows the accumulation of NOGGIN mRNA that will be further translated to inhibit BMP pathway activity (9) and to trigger the dedifferentiation of the SMCs (A). Disruption of RBPMS2 homodimerization through Leu to Glu substitution in position 49 leads to monomeric RBPMS2 proteins unable to interact with eEF2 and inefficient to induce the dedifferentiation process (B).

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).


Homodimerization of RBPMS2 through a new RRM-interaction motif is necessary to control smooth muscle plasticity.

Sagnol S, Yang Y, Bessin Y, Allemand F, Hapkova I, Notarnicola C, Guichou JF, Faure S, Labesse G, de Santa Barbara P - Nucleic Acids Res. (2014)

Model of the action of RBPMS2 homodimerization in the SMC dedifferentiation process. Homodimeric RBPMS2 complex interacts with eEF2, an essential member of the eukaryote translational machinery that allows the accumulation of NOGGIN mRNA that will be further translated to inhibit BMP pathway activity (9) and to trigger the dedifferentiation of the SMCs (A). Disruption of RBPMS2 homodimerization through Leu to Glu substitution in position 49 leads to monomeric RBPMS2 proteins unable to interact with eEF2 and inefficient to induce the dedifferentiation process (B).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4150794&req=5

Figure 6: Model of the action of RBPMS2 homodimerization in the SMC dedifferentiation process. Homodimeric RBPMS2 complex interacts with eEF2, an essential member of the eukaryote translational machinery that allows the accumulation of NOGGIN mRNA that will be further translated to inhibit BMP pathway activity (9) and to trigger the dedifferentiation of the SMCs (A). Disruption of RBPMS2 homodimerization through Leu to Glu substitution in position 49 leads to monomeric RBPMS2 proteins unable to interact with eEF2 and inefficient to induce the dedifferentiation process (B).
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).

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.

View Article: PubMed Central - PubMed

Affiliation: INSERM U1046, Université Montpellier 1, Université Montpellier 2, 34295 Montpellier, France.

Show MeSH
Related in: MedlinePlus