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The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions

In Myxococcus xanthus the gliding motility machinery is assembled at the leading cell pole to form focal adhesions, translocated rearward to propel the cell, and disassembled at the lagging pole. We show that MglA, a Ras-like small G-protein, is an integral part of this machinery. In this function,...

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Autores principales: Treuner-Lange, Anke, Macia, Eric, Guzzo, Mathilde, Hot, Edina, Faure, Laura M., Jakobczak, Beata, Espinosa, Leon, Alcor, Damien, Ducret, Adrien, Keilberg, Daniela, Castaing, Jean Philippe, Lacas Gervais, Sandra, Franco, Michel, Søgaard-Andersen, Lotte, Mignot, Tâm
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4508894/
https://www.ncbi.nlm.nih.gov/pubmed/26169353
http://dx.doi.org/10.1083/jcb.201412047
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author Treuner-Lange, Anke
Macia, Eric
Guzzo, Mathilde
Hot, Edina
Faure, Laura M.
Jakobczak, Beata
Espinosa, Leon
Alcor, Damien
Ducret, Adrien
Keilberg, Daniela
Castaing, Jean Philippe
Lacas Gervais, Sandra
Franco, Michel
Søgaard-Andersen, Lotte
Mignot, Tâm
author_facet Treuner-Lange, Anke
Macia, Eric
Guzzo, Mathilde
Hot, Edina
Faure, Laura M.
Jakobczak, Beata
Espinosa, Leon
Alcor, Damien
Ducret, Adrien
Keilberg, Daniela
Castaing, Jean Philippe
Lacas Gervais, Sandra
Franco, Michel
Søgaard-Andersen, Lotte
Mignot, Tâm
author_sort Treuner-Lange, Anke
collection PubMed
description In Myxococcus xanthus the gliding motility machinery is assembled at the leading cell pole to form focal adhesions, translocated rearward to propel the cell, and disassembled at the lagging pole. We show that MglA, a Ras-like small G-protein, is an integral part of this machinery. In this function, MglA stimulates the assembly of the motility complex by directly connecting it to the MreB actin cytoskeleton. Because the nucleotide state of MglA is regulated spatially and MglA only binds MreB in the guanosine triphosphate–bound form, the motility complexes are assembled at the leading pole and dispersed at the lagging pole where the guanosine triphosphatase activating protein MglB disrupts the MglA–MreB interaction. Thus, MglA acts as a nucleotide-dependent molecular switch to regulate the motility machinery spatially. The function of MreB in motility is independent of its function in peptidoglycan synthesis, representing a coopted function. Our findings highlight a new function for the MreB cytoskeleton and suggest that G-protein–cytoskeleton interactions are a universally conserved feature.
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spelling pubmed-45088942016-01-20 The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions Treuner-Lange, Anke Macia, Eric Guzzo, Mathilde Hot, Edina Faure, Laura M. Jakobczak, Beata Espinosa, Leon Alcor, Damien Ducret, Adrien Keilberg, Daniela Castaing, Jean Philippe Lacas Gervais, Sandra Franco, Michel Søgaard-Andersen, Lotte Mignot, Tâm J Cell Biol Research Articles In Myxococcus xanthus the gliding motility machinery is assembled at the leading cell pole to form focal adhesions, translocated rearward to propel the cell, and disassembled at the lagging pole. We show that MglA, a Ras-like small G-protein, is an integral part of this machinery. In this function, MglA stimulates the assembly of the motility complex by directly connecting it to the MreB actin cytoskeleton. Because the nucleotide state of MglA is regulated spatially and MglA only binds MreB in the guanosine triphosphate–bound form, the motility complexes are assembled at the leading pole and dispersed at the lagging pole where the guanosine triphosphatase activating protein MglB disrupts the MglA–MreB interaction. Thus, MglA acts as a nucleotide-dependent molecular switch to regulate the motility machinery spatially. The function of MreB in motility is independent of its function in peptidoglycan synthesis, representing a coopted function. Our findings highlight a new function for the MreB cytoskeleton and suggest that G-protein–cytoskeleton interactions are a universally conserved feature. The Rockefeller University Press 2015-07-20 /pmc/articles/PMC4508894/ /pubmed/26169353 http://dx.doi.org/10.1083/jcb.201412047 Text en © 2015 Treuner-Lange et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Treuner-Lange, Anke
Macia, Eric
Guzzo, Mathilde
Hot, Edina
Faure, Laura M.
Jakobczak, Beata
Espinosa, Leon
Alcor, Damien
Ducret, Adrien
Keilberg, Daniela
Castaing, Jean Philippe
Lacas Gervais, Sandra
Franco, Michel
Søgaard-Andersen, Lotte
Mignot, Tâm
The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions
title The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions
title_full The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions
title_fullStr The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions
title_full_unstemmed The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions
title_short The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions
title_sort small g-protein mgla connects to the mreb actin cytoskeleton at bacterial focal adhesions
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4508894/
https://www.ncbi.nlm.nih.gov/pubmed/26169353
http://dx.doi.org/10.1083/jcb.201412047
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