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Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking

The small Rho-family GTPase Cdc42 is critical for cell polarization and polarizes spontaneously in absence of upstream spatial cues. Spontaneous polarization is thought to require dynamic Cdc42 recycling through Guanine nucleotide Dissociation Inhibitor (GDI)-mediated membrane extraction and vesicle...

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Detalles Bibliográficos
Autores principales: Bendezú, Felipe O., Vincenzetti, Vincent, Vavylonis, Dimitrios, Wyss, Romain, Vogel, Horst, Martin, Sophie G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383620/
https://www.ncbi.nlm.nih.gov/pubmed/25837586
http://dx.doi.org/10.1371/journal.pbio.1002097
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author Bendezú, Felipe O.
Vincenzetti, Vincent
Vavylonis, Dimitrios
Wyss, Romain
Vogel, Horst
Martin, Sophie G.
author_facet Bendezú, Felipe O.
Vincenzetti, Vincent
Vavylonis, Dimitrios
Wyss, Romain
Vogel, Horst
Martin, Sophie G.
author_sort Bendezú, Felipe O.
collection PubMed
description The small Rho-family GTPase Cdc42 is critical for cell polarization and polarizes spontaneously in absence of upstream spatial cues. Spontaneous polarization is thought to require dynamic Cdc42 recycling through Guanine nucleotide Dissociation Inhibitor (GDI)-mediated membrane extraction and vesicle trafficking. Here, we describe a functional fluorescent Cdc42 allele in fission yeast, which demonstrates Cdc42 dynamics and polarization independent of these pathways. Furthermore, an engineered Cdc42 allele targeted to the membrane independently of these recycling pathways by an amphipathic helix is viable and polarizes spontaneously to multiple sites in fission and budding yeasts. We show that Cdc42 is highly mobile at the membrane and accumulates at sites of activity, where it displays slower mobility. By contrast, a near-immobile transmembrane domain-containing Cdc42 allele supports viability and polarized activity, but does not accumulate at sites of activity. We propose that Cdc42 activation, enhanced by positive feedback, leads to its local accumulation by capture of fast-diffusing inactive molecules.
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spelling pubmed-43836202015-04-09 Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking Bendezú, Felipe O. Vincenzetti, Vincent Vavylonis, Dimitrios Wyss, Romain Vogel, Horst Martin, Sophie G. PLoS Biol Research Article The small Rho-family GTPase Cdc42 is critical for cell polarization and polarizes spontaneously in absence of upstream spatial cues. Spontaneous polarization is thought to require dynamic Cdc42 recycling through Guanine nucleotide Dissociation Inhibitor (GDI)-mediated membrane extraction and vesicle trafficking. Here, we describe a functional fluorescent Cdc42 allele in fission yeast, which demonstrates Cdc42 dynamics and polarization independent of these pathways. Furthermore, an engineered Cdc42 allele targeted to the membrane independently of these recycling pathways by an amphipathic helix is viable and polarizes spontaneously to multiple sites in fission and budding yeasts. We show that Cdc42 is highly mobile at the membrane and accumulates at sites of activity, where it displays slower mobility. By contrast, a near-immobile transmembrane domain-containing Cdc42 allele supports viability and polarized activity, but does not accumulate at sites of activity. We propose that Cdc42 activation, enhanced by positive feedback, leads to its local accumulation by capture of fast-diffusing inactive molecules. Public Library of Science 2015-04-02 /pmc/articles/PMC4383620/ /pubmed/25837586 http://dx.doi.org/10.1371/journal.pbio.1002097 Text en © 2015 Bendezú et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Bendezú, Felipe O.
Vincenzetti, Vincent
Vavylonis, Dimitrios
Wyss, Romain
Vogel, Horst
Martin, Sophie G.
Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking
title Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking
title_full Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking
title_fullStr Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking
title_full_unstemmed Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking
title_short Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking
title_sort spontaneous cdc42 polarization independent of gdi-mediated extraction and actin-based trafficking
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383620/
https://www.ncbi.nlm.nih.gov/pubmed/25837586
http://dx.doi.org/10.1371/journal.pbio.1002097
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