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β1A Integrin Is a Master Regulator of Invadosome Organization and Function
Invadosomes are adhesion structures involved in tissue invasion that are characterized by an intense actin polymerization–depolymerization associated with β1 and β3 integrins and coupled to extracellular matrix (ECM) degradation activity. We induced the formation of invadosomes by expressing the con...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2993740/ https://www.ncbi.nlm.nih.gov/pubmed/20926684 http://dx.doi.org/10.1091/mbc.E10-07-0580 |
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author | Destaing, Olivier Planus, Emmanuelle Bouvard, Daniel Oddou, Christiane Badowski, Cedric Bossy, Valentine Raducanu, Aurelia Fourcade, Bertrand Albiges-Rizo, Corinne Block, Marc R. |
author_facet | Destaing, Olivier Planus, Emmanuelle Bouvard, Daniel Oddou, Christiane Badowski, Cedric Bossy, Valentine Raducanu, Aurelia Fourcade, Bertrand Albiges-Rizo, Corinne Block, Marc R. |
author_sort | Destaing, Olivier |
collection | PubMed |
description | Invadosomes are adhesion structures involved in tissue invasion that are characterized by an intense actin polymerization–depolymerization associated with β1 and β3 integrins and coupled to extracellular matrix (ECM) degradation activity. We induced the formation of invadosomes by expressing the constitutive active form of Src, SrcYF, in different cell types. Use of ECM surfaces micropatterned at the subcellular scale clearly showed that in mesenchymal cells, integrin signaling controls invadosome activity. Using β1(−/−) or β3(−/−) cells, it seemed that β1A but not β3 integrins are essential for initiation of invadosome formation. Protein kinase C activity was shown to regulate autoassembly of invadosomes into a ring-like metastructure (rosette), probably by phosphorylation of Ser785 on the β1A tail. Moreover, our study clearly showed that β1A links actin dynamics and ECM degradation in invadosomes. Finally, a new strategy based on fusion of the photosensitizer KillerRed to the β1A cytoplasmic domain allowed specific and immediate loss of function of β1A, resulting in disorganization and disassembly of invadosomes and formation of focal adhesions. |
format | Text |
id | pubmed-2993740 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-29937402011-02-16 β1A Integrin Is a Master Regulator of Invadosome Organization and Function Destaing, Olivier Planus, Emmanuelle Bouvard, Daniel Oddou, Christiane Badowski, Cedric Bossy, Valentine Raducanu, Aurelia Fourcade, Bertrand Albiges-Rizo, Corinne Block, Marc R. Mol Biol Cell Articles Invadosomes are adhesion structures involved in tissue invasion that are characterized by an intense actin polymerization–depolymerization associated with β1 and β3 integrins and coupled to extracellular matrix (ECM) degradation activity. We induced the formation of invadosomes by expressing the constitutive active form of Src, SrcYF, in different cell types. Use of ECM surfaces micropatterned at the subcellular scale clearly showed that in mesenchymal cells, integrin signaling controls invadosome activity. Using β1(−/−) or β3(−/−) cells, it seemed that β1A but not β3 integrins are essential for initiation of invadosome formation. Protein kinase C activity was shown to regulate autoassembly of invadosomes into a ring-like metastructure (rosette), probably by phosphorylation of Ser785 on the β1A tail. Moreover, our study clearly showed that β1A links actin dynamics and ECM degradation in invadosomes. Finally, a new strategy based on fusion of the photosensitizer KillerRed to the β1A cytoplasmic domain allowed specific and immediate loss of function of β1A, resulting in disorganization and disassembly of invadosomes and formation of focal adhesions. The American Society for Cell Biology 2010-12-01 /pmc/articles/PMC2993740/ /pubmed/20926684 http://dx.doi.org/10.1091/mbc.E10-07-0580 Text en © 2010 by The American Society for Cell Biology This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). |
spellingShingle | Articles Destaing, Olivier Planus, Emmanuelle Bouvard, Daniel Oddou, Christiane Badowski, Cedric Bossy, Valentine Raducanu, Aurelia Fourcade, Bertrand Albiges-Rizo, Corinne Block, Marc R. β1A Integrin Is a Master Regulator of Invadosome Organization and Function |
title | β1A Integrin Is a Master Regulator of Invadosome Organization and Function |
title_full | β1A Integrin Is a Master Regulator of Invadosome Organization and Function |
title_fullStr | β1A Integrin Is a Master Regulator of Invadosome Organization and Function |
title_full_unstemmed | β1A Integrin Is a Master Regulator of Invadosome Organization and Function |
title_short | β1A Integrin Is a Master Regulator of Invadosome Organization and Function |
title_sort | β1a integrin is a master regulator of invadosome organization and function |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2993740/ https://www.ncbi.nlm.nih.gov/pubmed/20926684 http://dx.doi.org/10.1091/mbc.E10-07-0580 |
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