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Updated: Jul 28, 2025

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Two RhoGEF isoforms with distinct localisation control furrow position during asymmetric cell division.

Emilie Montembault1,2, Irène Deduyer1,2, Marie-Charlotte Claverie1,2

  • 1CNRS, UMR5095, University of Bordeaux, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33607, Pessac, France.

Nature Communications
|June 2, 2023
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Summary
This summary is machine-generated.

Two Pbl protein isoforms regulate Rho1 GTPase during asymmetric cell division. This ensures proper cleavage furrow positioning and daughter cell size, making cytokinesis more robust.

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Area of Science:

  • Cell Biology
  • Developmental Biology
  • Molecular Biology

Background:

  • Cytokinesis is crucial for cell division, relying on the acto-myosin contractile ring and cleavage furrow ingression.
  • Rho1 GTPase and its activator Pbl are essential for cytokinesis, but their precise regulation remains unclear.

Purpose of the Study:

  • To investigate how Rho1 GTPase is regulated during asymmetric division in Drosophila neuroblasts.
  • To understand the distinct roles of Pbl isoforms in controlling Rho1 activity and cytokinesis.

Main Methods:

  • Utilized Drosophila neuroblast asymmetric division models.
  • Investigated the localization and function of Pbl-A and Pbl-B isoforms.
  • Analyzed Rho1 activity and myosin distribution.

Main Results:

  • Two Pbl isoforms, Pbl-A and Pbl-B, exhibit distinct subcellular localizations.
  • Pbl-A at the spindle midzone and furrow sustains efficient furrow ingression.
  • Pbl-B at the plasma membrane broadens Rho1 activity, enriching myosin and adjusting furrow position for cell size asymmetry.

Conclusions:

  • Distinct Pbl isoforms differentially regulate Rho1 GTPase localization and activity.
  • This isoform-specific regulation ensures robust control of cleavage furrow positioning and daughter cell size asymmetry.
  • The study reveals a mechanism for enhancing cytokinesis fidelity through protein isoform diversity.