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Integrin activation and matrix binding mediate cellular responses to mechanical stretch.

Akira Katsumi·Tomoki Naoe·Tadashi Matsushita·Kozo Kaibuchi·Martin Alexander Schwartz
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Abstract

Mechanical tension is a critical determinant of cell growth, differentiation, apoptosis, migration, and development. Integrins have been implicated in sensing force but little is known about how forces are transduced to biochemical signals. We now show that mechanical strain stimulates conformational activation of integrin alphavbeta3 in NIH3T3 cells. Integrin activation is mediated by phosphoinositol 3-kinase and is followed by an increase in integrin binding to extracellular matrix proteins. Mechanical stretch stimulation of JNK was dependent on new integrin binding to extracellular matrix. These data define a molecular mechanism for the role of integrins in mechanotransduction.

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AnimalsCell AdhesionEnzyme ActivationEnzyme InhibitorsExtracellular MatrixExtracellular Signal-Regulated MAP KinasesIntegrin alphaVbeta3IntegrinsJNK Mitogen-Activated Protein KinasesLigandsMAP Kinase Kinase 4MiceMitogen-Activated Protein Kinase KinasesNIH 3T3 CellsPhosphatidylinositol 3-KinasesPhosphorylationProtein ConformationSignal TransductionStress, MechanicalTime FactorsJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, U.S. Gov't, P.H.S.

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Akira Katsumi, Tomoki Naoe, Tadashi Matsushita, Kozo Kaibuchi, Martin Alexander Schwartz. 2005-03-10. Integrin activation and matrix binding mediate cellular responses to mechanical stretch.. https://doi.org/10.1074/jbc.c400455200

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