Journal
LIFE-BASEL
Volume 11, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/life11111147
Keywords
PRMT1; arginine methylation; transcriptional regulation; cell signaling; DNA damage repair; cancer
Categories
Funding
- La Ligue contre le Cancer
- Fondation ARC Cancer
- Fondation de France
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PRMT1, the major protein arginine methyltransferase in mammals, plays essential roles in various biological processes such as transcriptional regulation, signal transduction, and DNA repair. It catalyzes monomethylation and asymmetric dimethylation of arginine side chains in proteins, with a wide range of substrates identified including histone and non-histone proteins. The enzyme is also involved in embryonic development, DNA damage repair, and the progression of various cancers.
PRMT1, the major protein arginine methyltransferase in mammals, catalyzes monomethylation and asymmetric dimethylation of arginine side chains in proteins. Initially described as a regulator of chromatin dynamics through the methylation of histone H4 at arginine 3 (H4R3), numerous non-histone substrates have since been identified. The variety of these substrates underlines the essential role played by PRMT1 in a large number of biological processes such as transcriptional regulation, signal transduction or DNA repair. This review will provide an overview of the structural, biochemical and cellular features of PRMT1. After a description of the genomic organization and protein structure of PRMT1, special consideration was given to the regulation of PRMT1 enzymatic activity. Finally, we discuss the involvement of PRMT1 in embryonic development, DNA damage repair, as well as its participation in the initiation and progression of several types of cancers.
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