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The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly
Focal adhesions (FA) are a complex network of proteins that allow the cell to form physical contacts with the extracellular matrix (ECM). FA assemble and disassemble in a dynamic process, orchestrated by a variety of cellular components. However, the underlying mechanisms that regulate adhesion turn...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6435757/ https://www.ncbi.nlm.nih.gov/pubmed/30914742 http://dx.doi.org/10.1038/s41598-019-41558-7 |
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author | Zinn, Ashtyn Goicoechea, Silvia M. Kreider-Letterman, Gabriel Maity, Debonil Awadia, Sahezeel Cedeno-Rosario, Luis Chen, Yun Garcia-Mata, Rafael |
author_facet | Zinn, Ashtyn Goicoechea, Silvia M. Kreider-Letterman, Gabriel Maity, Debonil Awadia, Sahezeel Cedeno-Rosario, Luis Chen, Yun Garcia-Mata, Rafael |
author_sort | Zinn, Ashtyn |
collection | PubMed |
description | Focal adhesions (FA) are a complex network of proteins that allow the cell to form physical contacts with the extracellular matrix (ECM). FA assemble and disassemble in a dynamic process, orchestrated by a variety of cellular components. However, the underlying mechanisms that regulate adhesion turnover remain poorly understood. Here we show that RhoG, a Rho GTPase related to Rac, modulates FA dynamics. When RhoG expression is silenced, FA are more stable and live longer, resulting in an increase in the number and size of adhesions, which are also more mature and fibrillar-like. Silencing RhoG also increases the number and thickness of stress fibers, which are sensitive to blebbistatin, suggesting contractility is increased. The molecular mechanism by which RhoG regulates adhesion turnover is yet to be characterized, but our results demonstrate that RhoG plays a role in the regulation of microtubule-mediated FA disassembly. |
format | Online Article Text |
id | pubmed-6435757 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-64357572019-04-03 The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly Zinn, Ashtyn Goicoechea, Silvia M. Kreider-Letterman, Gabriel Maity, Debonil Awadia, Sahezeel Cedeno-Rosario, Luis Chen, Yun Garcia-Mata, Rafael Sci Rep Article Focal adhesions (FA) are a complex network of proteins that allow the cell to form physical contacts with the extracellular matrix (ECM). FA assemble and disassemble in a dynamic process, orchestrated by a variety of cellular components. However, the underlying mechanisms that regulate adhesion turnover remain poorly understood. Here we show that RhoG, a Rho GTPase related to Rac, modulates FA dynamics. When RhoG expression is silenced, FA are more stable and live longer, resulting in an increase in the number and size of adhesions, which are also more mature and fibrillar-like. Silencing RhoG also increases the number and thickness of stress fibers, which are sensitive to blebbistatin, suggesting contractility is increased. The molecular mechanism by which RhoG regulates adhesion turnover is yet to be characterized, but our results demonstrate that RhoG plays a role in the regulation of microtubule-mediated FA disassembly. Nature Publishing Group UK 2019-03-26 /pmc/articles/PMC6435757/ /pubmed/30914742 http://dx.doi.org/10.1038/s41598-019-41558-7 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Zinn, Ashtyn Goicoechea, Silvia M. Kreider-Letterman, Gabriel Maity, Debonil Awadia, Sahezeel Cedeno-Rosario, Luis Chen, Yun Garcia-Mata, Rafael The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly |
title | The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly |
title_full | The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly |
title_fullStr | The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly |
title_full_unstemmed | The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly |
title_short | The small GTPase RhoG regulates microtubule-mediated focal adhesion disassembly |
title_sort | small gtpase rhog regulates microtubule-mediated focal adhesion disassembly |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6435757/ https://www.ncbi.nlm.nih.gov/pubmed/30914742 http://dx.doi.org/10.1038/s41598-019-41558-7 |
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