Versatility of PRMT5-induced methylation in growth control and development

UMMS Affiliation

Department of Cell Biology

Publication Date


Document Type



Protein-Arginine N-Methyltransferases


Cell Biology


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.

DOI of Published Version



Trends Biochem Sci. 2011 Dec;36(12):633-41. Epub 2011 Oct 3. Link to article on publisher's site

Journal/Book/Conference Title

Trends in biochemical sciences

Related Resources

Link to Article in PubMed

PubMed ID