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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...

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Autores principales: Zinn, Ashtyn, Goicoechea, Silvia M., Kreider-Letterman, Gabriel, Maity, Debonil, Awadia, Sahezeel, Cedeno-Rosario, Luis, Chen, Yun, Garcia-Mata, Rafael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
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.
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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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