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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,...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2015
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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. |
format | Online Article Text |
id | pubmed-4508894 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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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