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; PRMT inhibitor; arginine methylation; cancer; epigenetic modifications; non-histone protein.
Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.
MeSH terms
-
Antineoplastic Agents / therapeutic use
-
Arginine / metabolism*
-
Cardiovascular Diseases / enzymology*
-
Cardiovascular Diseases / genetics
-
Cardiovascular Diseases / pathology
-
Enzyme Inhibitors / therapeutic use
-
Epigenesis, Genetic
-
Histones / genetics
-
Histones / metabolism
-
Humans
-
Metabolic Diseases / enzymology*
-
Metabolic Diseases / genetics
-
Metabolic Diseases / pathology
-
Methylation
-
Neoplasms / drug therapy
-
Neoplasms / enzymology*
-
Neoplasms / genetics
-
Neoplasms / pathology
-
Protein Processing, Post-Translational*
-
Protein-Arginine N-Methyltransferases / antagonists & inhibitors
-
Protein-Arginine N-Methyltransferases / classification
-
Protein-Arginine N-Methyltransferases / genetics
-
Protein-Arginine N-Methyltransferases / metabolism*
-
RNA Splicing
-
Signal Transduction
-
Transcription Factors / antagonists & inhibitors
-
Transcription Factors / classification
-
Transcription Factors / genetics
-
Transcription Factors / metabolism*
Substances
-
Antineoplastic Agents
-
Enzyme Inhibitors
-
Histones
-
Transcription Factors
-
Arginine
-
Protein-Arginine N-Methyltransferases