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Non-Histone Arginine Methylation by Protein Arginine Methyltransferases

Ayad A. Al-Hamashi, Krystal Diaz, Rong Huang

2020Current Protein and Peptide Science58 citationsDOIOpen Access PDF

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.

Topics & Concepts

Protein arginine methyltransferase 5Histone methyltransferaseHistoneMethyltransferaseArginineMethylationHistone methylationBiologyRNA splicingEZH2EpigenomicsBiochemistryAlternative splicingCell biologyDNA methylationGene expressionDNAGeneRNAMessenger RNAAmino acidCancer-related gene regulationEpigenetics and DNA Methylation
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