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Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex.

Lukasz Kozubowski1, Koji Saito, Jayme M Johnson

  • 1Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.

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The scaffold protein Bem1p facilitates cell polarization by forming a complex with a guanine nucleotide exchange factor (GEF) and a p21-activated kinase (PAK). This complex amplifies Cdc42p activity, driving symmetry breaking in yeast cells.

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Area of Science:

  • Cell biology
  • Developmental biology
  • Biophysics

Background:

  • Symmetry breaking, a form of self-organization, leads to cell polarization without external cues.
  • The GTPase Cdc42p is crucial for cell polarization, concentrating at a specific cortical site.
  • The scaffold protein Bem1p is required for Cdc42p concentration during symmetry breaking, but its mechanism was unclear.

Purpose of the Study:

  • To elucidate the mechanism by which Bem1p promotes symmetry breaking and cell polarization.
  • To investigate the role of the GEF and PAK proteins in Bem1p-mediated polarization.

Main Methods:

  • Analysis of Bem1p mutants to determine the binding requirements of GEF and PAK.
  • Construction of a protein fusion linking GEF and PAK to bypass Bem1p.
  • Engineering an artificial GEF in yeast to mimic mammalian multidomain GEFs.

Main Results:

  • Bem1p assembles a complex containing both a Cdc42p-directed GEF and a PAK.
  • Both GEF and PAK must bind to the same Bem1p molecule for symmetry breaking.
  • A protein fusion of GEF and PAK can promote symmetry breaking independently of Bem1p.
  • An artificial GEF with mammalian-like architecture can induce symmetry breaking in yeast without Bem1p.

Conclusions:

  • Yeast cell polarization via symmetry breaking involves a GEF-PAK complex.
  • This complex binds GTP-Cdc42p via PAK and enhances local GTP-loading via GEF.
  • The complex amplifies GTP-Cdc42p clusters, providing mechanistic insight into conserved pattern-forming pathways.