title: Histone arginine methylations: their roles in chromatin dynamics and transcriptional regulation.
abstract: PRMTs (protein arginine N-methyltransferases) specifically modify the arginine residues of key cellular and nuclear proteins as well as histone substrates. Like lysine methylation, transcriptional repression or activation is dependent upon the site and type of arginine methylation on histone tails. Recent discoveries imply that histone arginine methylation is an important modulator of dynamic chromatin regulation and transcriptional controls. However, under the shadow of lysine methylation, the roles of histone arginine methylation have been under-explored. The present review focuses on the roles of histone arginine methylation in the regulation of gene expression, and the interplays between histone arginine methylation, histone acetylation, lysine methylation and chromatin remodelling factors. In addition, we discuss the dynamic regulation of arginine methylation by arginine demethylases, and how dysregulation of PRMTs and their activities are linked to human diseases such as cancer.
authors.affiliation: Medical Education Center, Ball State University, Muncie, IN 47302, USA.
authors.forename: Michael
authors.initials: M
authors.lastname: Litt
authors.forename: Yi
authors.initials: Y
authors.lastname: Qiu
authors.forename: Suming
authors.initials: S
authors.lastname: Huang
mesh_terms: D001120:Arginine / Q000737:chemistry*; D002843:Chromatin / Q000378:metabolism*; D005786:Gene Expression Regulation; D006657:Histones / Q000737:chemistry*; D008745:Methylation; D008954:Models, Biological; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D002843:Chromatin; D006657:Histones; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases