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The cytokinesis regulator RacGAP1 is a Rac1-specific GAP on membranes.

Pavlina Dubois1, Yann Ferrandez1, Clara Rey1

  • 1CNRS, Ecole Normale Superieure Paris-Saclay, Université Paris-Saclay, Gif-sur-Yvette, France.

Protein Science : a Publication of the Protein Society
|February 12, 2026
PubMed
Summary
This summary is machine-generated.

RacGAP1, a key regulator of cell division, requires specific membrane lipids like PS and PIP2 for its function. This study confirms RacGAP1 selectively inactivates Rac1 GTPase on membranes, crucial for cytokinesis.

Keywords:
GTP hydrolysisRac1RacGAP1Rho GTPasescytokinesismembraneprotein‐membrane interactionspecificity

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Rho family GTPases are critical for cytokinesis.
  • RacGAP1 is a major regulator of this process, but its substrate specificity and membrane-dependent activity were debated.
  • GTPase-activating proteins (GAPs) typically function on cell membranes.

Purpose of the Study:

  • To investigate the membrane-binding requirements and activity of RacGAP1.
  • To determine the specific Rho GTPase substrate inactivated by RacGAP1 in a membrane environment.
  • To elucidate the structural basis for RacGAP1's substrate specificity.

Main Methods:

  • Reconstitution of RacGAP1 activity using liposomes and purified proteins.
  • Fluorescence-based kinetic assays to measure GTPase-activating protein activity.
  • X-ray crystallography of Rac1-GDP-Pi complex and mutagenesis studies.

Main Results:

  • Phosphatidylserine (PS) and phosphoinositide 4,5-bisphosphate (PIP2) are essential lipids for RacGAP1 membrane binding.
  • Membranes potentiate the GTPase-activating activity of RacGAP1 towards Rac1.
  • RacGAP1 demonstrates high specificity for Rac1, with switch 1 and insert regions being key determinants.
  • A structural model suggests Rac1-RacGAP1 complex binding to the membrane facilitates Rac1 removal.

Conclusions:

  • RacGAP1 requires specific membrane lipids for binding and activity.
  • RacGAP1 functions as a Rac1-specific GAP on membranes, contributing to efficient Rac1 inactivation during cytokinesis.
  • Structural insights reveal determinants of RacGAP1's specificity for Rac1.