Title:Non-Histone Arginine Methylation by Protein Arginine Methyltransferases
VOLUME: 21 ISSUE: 7
Author(s):Ayad A. Al-Hamashi, Krystal Diaz and Rong Huang*
Affiliation:Department of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, Department of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, Department of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907
Keywords:PRMT, arginine methylation, non-histone protein, PRMT inhibitor, cancer, epigenetic modifications.
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.
