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  11. Prmt5-mediated Arginine Methylation Of Fxr1 Is Essential For Rna Binding In Cancer Cells.
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  3. Research Domains
  5. Engineering
  7. Environmental Engineering
  9. Air Pollution Modelling And Control
  11. Prmt5-mediated Arginine Methylation Of Fxr1 Is Essential For Rna Binding In Cancer Cells.

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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
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PRMT5-mediated arginine methylation of FXR1 is essential for RNA binding in cancer cells.

Anitha Vijayakumar1,2, Mrinmoyee Majumder1, Shasha Yin1

  • 1Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.

Nucleic Acids Research
|May 6, 2024

View abstract on PubMed

Summary
This summary is machine-generated.

Arginine methylation of FXR1 protein enhances its binding to G-quadruplex RNA structures, promoting cancer cell growth. PRMT5 enzyme is crucial for this methylation, impacting FXR1 stability and gene expression in oral cancer.

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Cancer Research

Background:

  • Arginine methylation stabilizes arginine-glycine-rich (RGG) motif-containing RNA-binding proteins (RBPs), influencing gene expression.
  • FXR1, an RBP, undergoes post-translational modification affecting its role in cancer cell growth and proliferation.

Purpose of the Study:

  • To investigate the role of FXR1 post-translational modification in mRNA binding and cancer cell proliferation.
  • To elucidate the mechanism by which FXR1 interacts with G-quadruplex (G4) RNA structures.
  • To determine the involvement of PRMT5 in FXR1 methylation and its downstream effects.

Main Methods:

  • Site-directed mutagenesis to identify key arginine residues in FXR1.
  • In vitro and in vivo assays to assess FXR1 methylation by PRMT5.
  • Enhanced crosslinking and immunoprecipitation (eCLIP) to identify FXR1-bound mRNAs.
  • Lithium chloride treatment to disrupt G4-RNA structures.

    • Main Results:

    • Mutations in FXR1's nuclear export signal and RGG domains abolished its binding to G4-RNAs.
    • PRMT5 inhibition reduced FXR1 methylation, protein stability, and RNA-binding activity, suppressing cancer cell growth.
    • FXR1 was found to bind G4-enriched mRNAs (e.g., AHNAK, MAP1B) and regulate their expression.

    Conclusions:

    • PRMT5-mediated arginine methylation of FXR1 is essential for its binding to G4-RNAs and subsequent promotion of gene expression in cancer cells.
    • FXR1's affinity for G4-RNA structures is a key factor in its function within oral cancer cells.
    • These findings offer new insights into the molecular mechanisms of FXR1 in oral cancer progression.