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Minireview: Protein Arginine Methylation of Nonhistone Proteins in Transcriptional Regulation

Department of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, California 90089

Address all correspondence and requests for reprints to: Michael R. Stallcup, Department of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, NOR 6316, 1441 Eastlake Avenue, Los Angeles, California 90089-9176. E-mail: stallcup{at}usc.edu.

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.

NURSA Molecule Pages Link:

Nuclear Receptors:   ERα

Coregulators:   PGC-1  |  BRM  |  BRG1  |  CARM1  |  PRMT2  |  PRMT1

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