Non-Histone Arginine Methylation by Protein Arginine Methyltransferases-Reference-Cited by-同舟云学术

Non-Histone Arginine Methylation by Protein Arginine Methyltransferases

Published:2020-09-23 Issue:7 Volume:21 Page:699-712
ISSN:1389-2037
Container-title:Current Protein & Peptide Science
language:en
Short-container-title:CPPS

Author:

Al-Hamashi Ayad A.¹,Diaz Krystal¹,Huang Rong¹^ORCID

Affiliation:

1. Department of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, United States

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.

Funder

National Institutes of Health

Publisher

Bentham Science Publishers Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,General Medicine

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