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Current Protein & Peptide Science

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ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

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Review Article

Non-Histone Arginine Methylation by Protein Arginine Methyltransferases

Author(s): Ayad A. Al-Hamashi, Krystal Diaz and Rong Huang*

Volume 21, Issue 7, 2020

Page: [699 - 712] Pages: 14

DOI: 10.2174/1389203721666200507091952

Price: $65

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: PRMT, arginine methylation, non-histone protein, PRMT inhibitor, cancer, epigenetic modifications.

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