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Related Experiment Video

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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
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Protein arginine methyltransferase 7-mediated arginine mono-methylation stabilizes SRY-box transcription factor 9 to

Lin Zhang1, Jingyi Xiang1, Yali Feng1,2

  • 1Key Laboratory of Molecular Biology for Infectious Diseases (Ministry of Education), Institute for Viral Hepatitis, Department of Infectious Diseases, The Second Affiliated Hospital, Chongqing Medical University, Chongqing, 400010, People's Republic of China.

Molecular Biomedicine
|December 22, 2025
PubMed
Summary

Protein arginine methyltransferase 7 (PRMT7) stabilizes the oncoprotein SOX9 in non-small cell lung cancer (NSCLC) by preventing its degradation. This PRMT7-SOX9 interaction promotes cancer growth and indicates a potential therapeutic target.

Keywords:
Arginine mono-methylationNon-small cell lung cancerProtein arginine methyltransferase 7SRY-Box transcription factor 9

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Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • Non-small cell lung cancer (NSCLC) is a major cause of cancer mortality globally.
  • SRY-box transcription factor 9 (SOX9) is an oncoprotein involved in NSCLC pathogenesis.
  • Post-translational regulation of SOX9 stability, especially by arginine methyltransferases, is not well understood.

Purpose of the Study:

  • To identify novel regulators of SOX9 stability in NSCLC.
  • To investigate the role of protein arginine methyltransferase 7 (PRMT7) in SOX9 regulation.
  • To explore the therapeutic potential of targeting the PRMT7-SOX9 axis in NSCLC.

Main Methods:

  • Protein-protein interaction assays to confirm PRMT7 and SOX9 binding.
  • Methylation assays to identify the specific site and type of SOX9 modification by PRMT7.
  • Ubiquitination and degradation assays to assess the impact of PRMT7 on SOX9 stability.
  • In vitro and in vivo functional assays to evaluate the role of PRMT7 in NSCLC proliferation and tumorigenesis.
  • Clinical analysis of PRMT7 and SOX9 expression in NSCLC patient samples.

Main Results:

  • PRMT7 directly interacts with SOX9 and enhances its stability in a methyltransferase-dependent manner.
  • PRMT7 catalyzes mono-methylation of SOX9 at R160, inhibiting its ubiquitination and proteasomal degradation by FBXW7 and KEAP1.
  • PRMT7 promotes NSCLC cell proliferation and tumorigenesis via SOX9.
  • PRMT7 and SOX9 are co-upregulated in NSCLC tissues, and high levels correlate with poorer patient survival.

Conclusions:

  • PRMT7 is a novel regulator of SOX9 stability and function in NSCLC.
  • The PRMT7-mediated methylation of SOX9 at R160 is a key mechanism for SOX9 stabilization.
  • The PRMT7-SOX9 axis represents a promising therapeutic target for NSCLC treatment.