Identification and characterization of human Mex-3 proteins, a novel family of evolutionarily conserved RNA-binding proteins differentially localized to processing bodies.
Fiche publication
Date publication
janvier 2007
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DOMON-DELL Claire, Dr FREUND Jean-Noël
Tous les auteurs :
Buchet-Poyau K, Courchet J, Le Hir H, Seraphin B, Scoazec JY, Duret L, Domon-Dell C, Freund JN, Billaud M
Lien Pubmed
Résumé
In Caenorhabditis elegans, the Mex-3 protein is a translational regulator that specifies the posterior blastomere identity in the early embryo and contributes to the maintenance of the germline totipotency. We have now identified a family of four homologous human Mex-3 genes, called hMex-3A to -3D that encode proteins containing two heterogeneous nuclear ribonucleoprotein K homology (KH) domains and one carboxy-terminal RING finger module. The hMex-3 are phosphoproteins that bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. Our analysis further revealed that hMex-3A and hMex-3B, but not hMex-3C, colocalize with both the hDcp1a decapping factor and Argonaute (Ago) proteins in processing bodies (P bodies), recently characterized as centers of mRNA turnover. Taken together, these findings indicate that hMex-3 proteins constitute a novel family of evolutionarily conserved RNA-binding proteins, differentially recruited to P bodies and potentially involved in post-transcriptional regulatory mechanisms.
Référence
Nucleic Acids Res. 2007;35(4):1289-300