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Updated: Jan 31, 2026

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Avidity-driven polarity establishment via multivalent lipid-GTPase module interactions.

Julien Meca1, Aurélie Massoni-Laporte1, Denis Martinez2

  • 1CNRS, UMR 5095, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France.

The EMBO Journal
|December 19, 2018
PubMed
Summary
This summary is machine-generated.

Multivalent lipid interactions drive cell polarity by controlling Rho GTPase activation. This avidity mechanism, involving the scaffold protein Bem1, is crucial for spatial signaling and cell polarization.

Keywords:
Rho GTPasecell polaritylipidsnanoclusteringsuper‐resolution imaging

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Rho GTPases are essential for cellular polarity.
  • Mechanisms of anisotropic Rho GTPase activation at membranes remain unclear.

Purpose of the Study:

  • Investigate the role of avidity in polarity establishment.
  • Elucidate the mechanisms of spatial control of GTPase activation at membranes.

Main Methods:

  • Utilized the budding yeast Cdc42 GTPase module (GEF Cdc24, scaffold Bem1).
  • Analyzed effects of mutations in Bem1 basic cluster motifs and domains.
  • Assessed Cdc42 nanoclustering and cellular polarity.

Main Results:

  • Avidity from multivalent anionic lipid interactions is critical for polarity.
  • Bem1 basic cluster motifs mediate scaffold-GEF complex interaction with anionic lipids.
  • Mutations disrupt Cdc42 nanoclustering, membrane properties, and cellular polarity.

Conclusions:

  • Avidity via multivalent anionic lipid interactions is a key mechanism for spatial GTPase activation.
  • This process regulates membrane properties and feedback signaling for polarity establishment.