Title
Versatility of PRMT5-induced methylation in growth control and development
UMMS Affiliation
Department of Cell Biology
Date
12-1-2011
Document Type
Article
Medical Subject Headings
Protein-Arginine N-Methyltransferases
Disciplines
Cell Biology
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.
Rights and Permissions
Citation: Trends Biochem Sci. 2011 Dec;36(12):633-41. Epub 2011 Oct 3. Link to article on publisher's site