Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2009 Apr;23(4):425-33.
doi: 10.1210/me.2008-0380. Epub 2009 Jan 22.

Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation

Affiliations
Review

Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation

Young-Ho Lee et al. Mol Endocrinol. 2009 Apr.

Abstract

Endocrine regulation frequently culminates in altered transcription of specific genes. The signal transduction pathways, which transmit the endocrine signal from cell surface to the transcription machinery, often involve posttranslational modifications of proteins. Although phosphorylation has been by far the most widely studied protein modification, recent studies have indicated important roles for other types of modification, including protein arginine methylation. Ten different protein arginine methyltransferase (PRMT) family members have been identified in mammalian cells, and numerous substrates are being identified for these PRMTs. Whereas major attention has been focused on the methylation of histones and its role in chromatin remodeling and transcriptional regulation, there are many nonhistone substrates methylated by PRMTs. This review primarily focuses on recent progress on the roles of the nonhistone protein methylation in transcription. Protein methylation of coactivators, transcription factors, and signal transducers, among other proteins, plays important roles in transcriptional regulation. Protein methylation may affect protein-protein interaction, protein-DNA or protein-RNA interaction, protein stability, subcellular localization, or enzymatic activity. Thus, protein arginine methylation is critical for regulation of transcription and potentially for various physiological/pathological processes.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Boffa LC, Karn J, Vidali G, Allfrey VG 1977 Distribution of NG, NG,-dimethylarginine in nuclear protein fractions. Biochem Biophys Res Commun 74:969–976 - PubMed
    1. Paik WK, Paik DC, Kim S 2007 Historical review: the field of protein methylation. Trends Biochem Sci 32:146–152 - PubMed
    1. Gary JD, Clarke S 1998 RNA and protein interactions modulated by protein arginine methylation. Prog Nucleic Acids Res Mol Biol 61:65–131 - PubMed
    1. McBride AE, Silver PA 2001 State of the arg: protein methylation at arginine comes of age. Cell 106:5–8 - PubMed
    1. Lee DY, Teyssier C, Strahl BD, Stallcup MR 2005 Role of protein methylation in regulation of transcription. Endocr Rev 26:147–170 - PubMed

Publication types

MeSH terms

Substances