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Cell Cycle. 2014;13(1):32-41. doi: 10.4161/cc.27353. Epub 2013 Dec 2.

Protein arginine methylation of non-histone proteins and its role in diseases.

Author information

1
Department of Pharmacology and Toxicology; Indiana University School of Medicine; Indianapolis, IN USA.
2
Department of Biochemistry and Molecular Biology; Indiana University School of Medicine; Indianapolis, IN USA.
3
Department of Pharmacology and Toxicology; Indiana University School of Medicine; Indianapolis, IN USA; Department of Biochemistry and Molecular Biology; Indiana University School of Medicine; Indianapolis, IN USA.

Abstract

Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate arginine residues on histones and other proteins. PRMTs play a crucial role in influencing various cellular functions, including cellular development and tumorigenesis. Arginine methylation by PRMTs is found on both nuclear and cytoplasmic proteins. Recently, there is increasing evidence regarding post-translational modifications of non-histone proteins by PRMTs, illustrating the previously unknown importance of PRMTs in the regulation of various cellular functions by post-translational modifications. In this review, we present the recent developments in the regulation of non-histone proteins by PRMTs.

KEYWORDS:

arginine; post-translational modification; protein arginine methyltransferases

PMID:
24296620
PMCID:
PMC3925732
DOI:
10.4161/cc.27353
[Indexed for MEDLINE]
Free PMC Article

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