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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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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. |
format | Online Article Text |
id | pubmed-4383620 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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