Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase.

Fiche publication


Date publication

novembre 2021

Journal

Life (Basel, Switzerland)

Auteurs

Membres identifiés du Cancéropôle Est :
Pr CAVARELLI Jean


Tous les auteurs :
Cura V, Cavarelli J

Résumé

PRMT2 belongs to the protein arginine methyltransferase (PRMT) family, which catalyzes the arginine methylation of target proteins. As a type I enzyme, PRMT2 produces asymmetric dimethyl arginine and has been shown to have weak methyltransferase activity on histone substrates in vitro, suggesting that its authentic substrates have not yet been found. PRMT2 contains the canonical PRMT methylation core and a unique Src homology 3 domain. Studies have demonstrated its clear implication in many different cellular processes. PRMT2 acts as a coactivator of several nuclear hormone receptors and is known to interact with a multitude of splicing-related proteins. Furthermore, PRMT2 is aberrantly expressed in several cancer types, including breast cancer and glioblastoma. These reports highlight the crucial role played by PRMT2 and the need for a better characterization of its activity and cellular functions.

Mots clés

PRMT2, SH3, cancer, epigenetics, protein arginine methylation

Référence

Life (Basel). 2021 Nov 19;11(11):