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- Title
Protein arginine methyltransferase 1, a major regulator of biological processes.
- Authors
Sudhakar, Sadhana R.N.; Khan, Shahper N.; Clark, Ariel; Hendrickson-Rebizant, Thordur; Patel, Shrinal; Lakowski, Ted M.; Davie, James R.
- Abstract
Protein arginine methyltransferase 1 (PRMT1) is a major type I arginine methyltransferase that catalyzes the formation of monomethyl and asymmetric dimethylarginine in protein substrates. It was first identified to asymmetrically methylate histone H4 at the third arginine residue forming the H4R3me2a active histone mark. However, several protein substrates are now identified as being methylated by PRMT1. As a result of its association with diverse classes of substrates, PRMT1 regulates several biological processes like chromatin dynamics, transcription, RNA processing, and signal transduction. The review provides an overview of PRMT1 structure, biochemical features, specificity, regulation, and role in cellular functions. We discuss the genomic distribution of PRMT1 and its association with tRNA genes. Further, we explore the different substrates of PRMT1 involved in splicing. In the end, we discuss the proteins that interact with PRMT1 and their downstream effects in diseased states.
- Subjects
PROTEIN arginine methyltransferases; PROTEINS; CELL physiology; CELLULAR signal transduction; ASYMMETRIC dimethylarginine; RNA splicing; METHYLTRANSFERASES
- Publication
Biochemistry & Cell Biology, 2024, Vol 102, Issue 2, p106
- ISSN
0829-8211
- Publication type
Article
- DOI
10.1139/bcb-2023-0212