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Updated: Dec 13, 2025

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
08:11

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

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PRMT5 function and targeting in cancer

Hyungsoo Kim1, Ze'ev A Ronai1

  • 1Cancer Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, 92037, USA.

Cell Stress
|August 4, 2020
PubMed

Insights

Protein arginine methyltransferase 5 (PRMT5) is crucial in cancer development and therapy response. Targeting PRMT5 offers a promising therapeutic strategy for various cancers.

Area of Science:

  • Oncology
  • Epigenetics
  • Molecular Biology

Background:

  • Protein methyl transferases are key regulators in cancer development, progression, and treatment response.
  • PRMT5, a member of the PRMT family, influences oncogenic processes.
  • PRMT5 impacts both tumor-intrinsic and microenvironmental signaling pathways.

Purpose of the Study:

  • To elucidate the multifaceted roles of PRMT5 in cancer.
  • To highlight PRMT5's influence on critical cellular processes relevant to oncogenesis.
  • To establish the therapeutic potential of targeting PRMT5 in cancer treatment.

Main Methods:

  • Review of existing literature on PRMT5 function in cancer.
  • Analysis of PRMT5's impact on histone and protein methylation.
  • Examination of PRMT5's role in RNA splicing, cell cycle, apoptosis, and metabolism.

Main Results:

  • PRMT5 regulates key oncogenic processes through epigenetic modifications and protein methylation.
  • PRMT5 affects vital cellular functions including RNA splicing, cell cycle control, cell death, and metabolic signaling.
  • Dysregulation of PRMT5 contributes to cancer development and progression.

Conclusions:

  • PRMT5 is a critical regulator in cancer, impacting multiple signaling pathways.
  • Understanding PRMT5's function provides a basis for developing targeted cancer therapies.
  • Targeting PRMT5 represents a viable therapeutic strategy for cancer treatment.
Keywords:
MEP50PRMT1PRMT5histonemethylationmethyltransferasesplicingtranscription

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