Non-Histone Arginine Methylation by Protein Arginine Methyltransferases

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

Journal Name: Current Protein & Peptide Science

Volume 21 , Issue 7 , 2020

Become EABM
Become Reviewer

Graphical Abstract:


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.

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 21
ISSUE: 7
Year: 2020
Page: [699 - 712]
Pages: 14
DOI: 10.2174/1389203721666200507091952
Price: $65

Article Metrics

PDF: 16