Non-Histone Arginine Methylation by Protein Arginine Methyltransferases
- 1 January 2020
- journal article
- review article
- Published by Bentham Science Publishers Ltd. in Current Protein & Peptide Science
- Vol. 21 (7), 699-712
- https://doi.org/10.2174/1389203721666200507091952
Abstract
Protein arginine methyltransferase (PRMT) enzymes play a crucial role in RNA splicing, DNA damage repair, cell signaling, and differentiation. Arginine methylation is a prominent posttransitional modification of histones and various non-histone proteins that can either activate or repress gene expression. The aberrant expression of PRMTs has been linked to multiple abnormalities, notably cancer. Herein, we review a number of non-histone protein substrates for all nine members of human PRMTs and how PRMT-mediated non-histone arginine methylation modulates various diseases. Additionally, we highlight the most recent clinical studies for several PRMT inhibitors.Keywords
Funding Information
- National Institutes of Health (R01GM117275 (R.H.), U01CA214649)
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