PRMT1 in human neoplasm: cancer biology and potential therapeutic target

Cell Commun Signal. 2024 Feb 8;22(1):102. doi: 10.1186/s12964-024-01506-z.

Abstract

Protein arginine methyltransferase 1 (PRMT1), the predominant type I protein arginine methyltransferase, plays a crucial role in normal biological functions by catalyzing the methylation of arginine side chains, specifically monomethylarginine (MMA) and asymmetric dimethylarginine (ADMA), within proteins. Recent investigations have unveiled an association between dysregulated PRMT1 expression and the initiation and progression of tumors, significantly impacting patient prognosis, attributed to PRMT1's involvement in regulating various facets of tumor cell biology, including DNA damage repair, transcriptional and translational regulation, as well as signal transduction. In this review, we present an overview of recent advancements in PRMT1 research across different tumor types, with a specific focus on its contributions to tumor cell proliferation, metastasis, invasion, and drug resistance. Additionally, we expound on the dynamic functions of PRMT1 during distinct stages of cancer progression, elucidating its unique regulatory mechanisms within the same signaling pathway and distinguishing between its promotive and inhibitory effects. Importantly, we sought to provide a comprehensive summary and analysis of recent research progress on PRMT1 in tumors, contributing to a deeper understanding of its role in tumorigenesis, development, and potential treatment strategies.

Keywords: Arginine methylation; Cancer biology; PRMT1; PRMT1 inhibitor; Target.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biology
  • Humans
  • Methylation
  • Neoplasms*
  • Protein Processing, Post-Translational*
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism
  • Repressor Proteins / metabolism

Substances

  • Protein-Arginine N-Methyltransferases
  • PRMT1 protein, human
  • Repressor Proteins