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Updated: Jul 28, 2025

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
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PRMT1 methylates METTL14 to modulate its oncogenic function

Jingchao Wang1, Zhen Wang1, Hiroyuki Inuzuka1

  • 1Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.

Neoplasia (New York, N.Y.)
|June 3, 2023
PubMed

Insights

Protein arginine methyltransferase 1 (PRMT1) methylates METTL14, a key component of the m6A writer complex. This arginine methylation regulates m6A modification and promotes cell proliferation, suggesting a role in tumorigenesis.

Area of Science:

  • Epigenetics
  • RNA biology
  • Cancer research

Background:

  • N6-methyladenosine (m6A) is a crucial mRNA modification regulating stability and splicing.
  • The METTL3-METTL14-WTAP complex catalyzes m6A, but its upstream regulation is poorly understood.
  • Post-translational modifications, particularly arginine methylation, are implicated in regulating protein function.

Purpose of the Study:

  • To investigate the role of protein arginine methyltransferases (PRMTs) in regulating the m6A writer complex.
  • To identify upstream regulators of METTL14 function at the post-translational level.
  • To elucidate the impact of METTL14 arginine methylation on m6A modification and cellular processes.

Main Methods:

  • Investigated the interaction between PRMT1 and METTL14.
  • Identified specific arginine residues on METTL14 methylated by PRMT1.
  • Assessed the functional consequences of METTL14 arginine methylation on m6A modification and cell proliferation.
  • Utilized the PRMT1 inhibitor MS023 to study the effects of methylation inhibition.

Main Results:

  • PRMT1 directly methylates arginine residues in the C-terminus of METTL14.
  • The reader protein SPF30 recognizes PRMT1-mediated arginine methylation on METTL14.
  • PRMT1-dependent arginine methylation of METTL14 is essential for m6A modification.
  • Arginine methylation of METTL14 promotes cell proliferation, an effect inhibited by MS023.

Conclusions:

  • PRMT1-mediated arginine methylation of METTL14 is a novel regulatory mechanism for m6A modification.
  • This modification plays a significant role in promoting cell proliferation and tumorigenesis.
  • Targeting PRMT1 could be a potential therapeutic strategy for cancers associated with aberrant m6A modification.
Keywords:
Arginine methylationMETTL14N6-methyladenosine (m6A)PRMT1

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