| Literature DB >> 32379587 |
Ayad A Al-Hamashi1, Krystal Diaz1, Rong Huang1.
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. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.Entities:
Keywords: PRMT; PRMT inhibitor; arginine methylation; cancer; epigenetic modifications; non-histone protein
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Year: 2020 PMID: 32379587 PMCID: PMC7529871 DOI: 10.2174/1389203721666200507091952
Source DB: PubMed Journal: Curr Protein Pept Sci ISSN: 1389-2037 Impact factor: 3.272