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Related Experiment Video

Updated: Jun 9, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
07:02

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

Published on: December 16, 2021

srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization.

Shaoshi Guo1, Shilai Bao

  • 1Key Laboratory of Molecular and Developmental Biology, Center for Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.

The Journal of Biological Chemistry
|September 3, 2010
PubMed
Summary

Protein arginine methyltransferase 5 (PRMT5) methylates srGAP2, a key regulator of neuronal migration. This arginine methylation influences srGAP2

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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
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Last Updated: Jun 9, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
07:02

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

Published on: December 16, 2021

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

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Neuroscience

Background:

  • Slit-Robo GTPase-activating proteins (srGAPs) are essential for neuronal migration by inhibiting Rho GTPases (Cdc42, Rac1, RhoA).
  • The precise regulatory mechanisms of srGAP2 function, particularly post-translational modifications, remain incompletely understood.

Purpose of the Study:

  • To investigate the interaction between srGAP2 and protein arginine methyltransferase 5 (PRMT5).
  • To elucidate the role of srGAP2 arginine methylation in regulating its cellular localization, function, and interaction dynamics.

Main Methods:

  • Co-immunoprecipitation assays to confirm physical interaction between srGAP2 and PRMT5.
  • Immunofluorescence microscopy to determine srGAP2 localization in response to PRMT5 activity.
  • Site-directed mutagenesis to create a methylation-deficient srGAP2 mutant (srGAP2-R927A).
  • Cell-based assays measuring cell adhesion, spreading, migration, and proliferation.

Main Results:

  • srGAP2 physically interacts with PRMT5, which binds to the N-terminus of srGAP2 (aa 225-538).
  • PRMT5 methylates srGAP2 at a C-terminal arginine residue (Arg-927).
  • The srGAP2-R927A methylation mutant exhibits impaired cell spreading, fails to localize to the leading edge of membrane protrusions, and disrupts srGAP2 homodimerization via the F-BAR domain.

Conclusions:

  • Arginine methylation of srGAP2 by PRMT5 is a critical post-translational modification regulating srGAP2 localization and function.
  • This methylation is essential for proper cell spreading and migration, likely by influencing membrane protrusion dynamics and srGAP2 homodimerization.