title: Versatility of PRMT5-induced methylation in growth control and development.
abstract: Arginine methylation governs important cellular processes that impact growth and proliferation, as well as differentiation and development. Through their ability to catalyze symmetric or asymmetric methylation of histone and non-histone proteins, members of the protein arginine methyltransferase (PRMT) family regulate chromatin structure and expression of a wide spectrum of target genes. Unlike other PRMTs, PRMT5 works in concert with a variety of cellular proteins including ATP-dependent chromatin remodelers and co-repressors to induce epigenetic silencing. Recent work also implicates PRMT5 in the control of growth-promoting and pro-survival pathways, which demonstrates its versatility as an enzyme involved in both epigenetic regulation of anti-cancer target genes and organelle biogenesis. These studies not only provide insight into the molecular mechanisms by which PRMT5 contributes to growth control, but also justify therapeutic targeting of PRMT5.
authors.affiliation: Department of Molecular and Cellular Biochemistry, College of Medicine, The Ohio State University, Columbus, OH 43210, USA.
authors.forename: Vrajesh
authors.initials: V
authors.lastname: Karkhanis
authors.forename: Yu-Jie
authors.initials: YJ
authors.lastname: Hu
authors.forename: Robert A
authors.initials: RA
authors.lastname: Baiocchi
authors.forename: Anthony N
authors.initials: AN
authors.lastname: Imbalzano
authors.forename: Saïd
authors.initials: S
authors.lastname: Sif
mesh_terms: D000818:Animals; D001120:Arginine / Q000378:metabolism; D002454:Cell Differentiation; D049109:Cell Proliferation; D047108:Embryonic Development; D006801:Humans; D008745:Methylation; D011496:Protein Methyltransferases / Q000235:genetics / Q000378:metabolism*; D011484:Protein-Arginine N-Methyltransferases
chemical_list: D001120:Arginine; D011496:Protein Methyltransferases; C400529:PRMT5 protein, human; D011484:Protein-Arginine N-Methyltransferases