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dc.contributor.authorKarkhanis, Vrajesh
dc.contributor.authorHu, Yu-Jie
dc.contributor.authorBaiocchi, Robert A.
dc.contributor.authorImbalzano, Anthony N.
dc.contributor.authorSif, Said
dc.date2022-08-11T08:09:08.000
dc.date.accessioned2022-08-23T16:18:36Z
dc.date.available2022-08-23T16:18:36Z
dc.date.issued2011-12-01
dc.date.submitted2012-03-28
dc.identifier.citationTrends Biochem Sci. 2011 Dec;36(12):633-41. Epub 2011 Oct 3. <a href="http://dx.doi.org/10.1016/j.tibs.2011.09.001">Link to article on publisher's site</a>
dc.identifier.issn0968-0004 (Linking)
dc.identifier.doi10.1016/j.tibs.2011.09.001
dc.identifier.pmid21975038
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34854
dc.description.abstractArginine 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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=21975038&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.tibs.2011.09.001
dc.subjectProtein-Arginine N-Methyltransferases
dc.subjectCell Biology
dc.titleVersatility of PRMT5-induced methylation in growth control and development
dc.typeJournal Article
dc.source.journaltitleTrends in biochemical sciences
dc.source.volume36
dc.source.issue12
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/imbalzano/14
dc.identifier.contextkey2706225
html.description.abstract<p>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.</p>
dc.identifier.submissionpathimbalzano/14
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages633-41


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