β1A integrin is a master regulator of invadosome organization and function
| Autor: | Aurelia Raducanu, Marc R. Block, Daniel Bouvard, Valentine Bossy, Cedric Badowski, Christiane Oddou, Bertrand Fourcade, Emmanuelle Planus, Corinne Albiges-Rizo, Olivier Destaing |
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| Přispěvatelé: | Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Dynamique des systèmes d'adhérence et différenciation (DySAD), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Department of Molecular Medicine [Martinsreid], Max Planck Institute of Biochemistry (MPIB), Max-Planck-Gesellschaft-Max-Planck-Gesellschaft, ANR PIRIBIO, ARC, ANR-07-MIME-0021,ROSETTE,Analyses sérologiques, fonctionnelles et structurales des facteurs de virulence, PfEMP1, impliqués dans le rosetting et l'auto-agglutinantion(2007) |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
MESH: Integrin beta3
MESH: Signal Transduction MESH: Antigens CD29 Podosome Polymerization Extracellular matrix Mesoderm Gene Knockout Techniques Mice 0302 clinical medicine Cell Movement MESH: Animals Cell Interactions Phosphorylation PKC MESH: Cell Movement Cells Cultured Protein Kinase C invadopodia MESH: Gene Knockout Techniques 0303 health sciences MESH: Mesoderm biology Cell adhesion molecule Integrin beta1 Integrin beta3 Articles invasion Cell biology Extracellular Matrix Genes src MESH: Polymerization 030220 oncology & carcinogenesis Invadopodia MESH: Cell Adhesion Molecules Proto-oncogene tyrosine-protein kinase Src Signal Transduction MESH: Cells Cultured Integrin [SDV.BC]Life Sciences [q-bio]/Cellular Biology MESH: Extracellular Matrix MESH: Actins Cell Membrane Structures MESH: Genes src MESH: Cell Adhesion Focal adhesion 03 medical and health sciences Cell Adhesion Animals Cell adhesion Molecular Biology MESH: Mice 030304 developmental biology Focal Adhesions MESH: Phosphorylation podosomes ECM degradation MESH: Focal Adhesions Cell Biology MESH: Protein Kinase C Actins MESH: Cell Membrane Structures biology.protein integrins Cell Adhesion Molecules |
| Zdroj: | Molecular Biology of the Cell Molecular Biology of the Cell, American Society for Cell Biology, 2010, 21 (23), pp.4108-19. ⟨10.1091/mbc.E10-07-0580⟩ |
| ISSN: | 1939-4586 |
| Popis: | Use of patterned surfaces, reverse genetics, and time-controlled photoinactivation showed that β1 but not β3 integrins are required for invadosome formation, self-assembly, and stabilization into a ring structure. The activation state of β1 as well as its phosphorylation by protein kinase C on Ser785 control these process and link to the degradative 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 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. |
| Databáze: | OpenAIRE |
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