Focal adhesion kinase-dependent regulation of adhesive forces involves vinculin recruitment to focal adhesions

Focal adhesion kinase-dependent regulation of adhesive forces involves vinculin recruitment to focal adhesions
Focal adhesion
kinase-dependent regulation of
adhesive forces involves
vinculin recruitment to focal
adhesions
Date de mise en ligne : vendredi 15 janvier 2010 - Présentation et annonces - Biology of the Cell - Dernières publications - Focal adhesion kinase-dependent regulation of adhesive forces involves vinculin recruitment to focal adhesions
Background information. FAK (focal adhesion kinase), an essential non-receptor tyrosine kinase, plays pivotal roles in migratory responses, adhesive signalling and mechanotransduction. FAK-dependent regulation of cell migration involves focal adhesion turnover dynamics as well as actin cytoskeleton polymerization and lamellipodia protrusion.
Whereas roles for FAK in migratory and mechanosensing responses have been established, the contribution of FAK to the generation of adhesive forces is not well understood.
Results. Using FAK-null cells expressing wild-type and mutant FAK under an inducible tetracycline promoter, we analysed the role of FAK in the generation of steady-state adhesive forces using micropatterned substrates and a hydrodynamic adhesion assay. FAK expression reduced steady-state strength by 30% compared with FAK-null cells.
FAK expression reduced VCL (vinculin) localization to focal adhesions by 35% independently of changes in integrin binding and localization of talin and paxillin. RNAi (RNA interference) knock-down of VCL abrogated the FAK-dependent differences in adhesive forces. FAK-dependent changes in VCL localization and adhesive forces were confirmed in human primary fibroblasts with FAK knocked down by RNAi. The autophosphorylation Tyr-397 and kinase domain Tyr-576/Tyr-577 sites were differentially required for FAK-mediated adhesive responses.
Conclusions. We demonstrate that FAK reduces steady-state adhesion strength by modulating VCL recruitment to focal adhesions. These findings provide insights into the role of FAK in mechanical interactions between a cell and Focal adhesion kinase-dependent regulation of adhesive forces involves vinculin recruitment to focal adhesions
Focal adhesion
kinase-dependent regulation of
adhesive forces involves
vinculin recruitment to focal
adhesions
Date de mise en ligne : vendredi 15 janvier 2010 - Présentation et annonces - Biology of the Cell - Dernières publications - Focal adhesion kinase-dependent regulation of adhesive forces involves vinculin recruitment to focal adhesions
Background information. FAK (focal adhesion kinase), an essential non-receptor tyrosine kinase, plays pivotal roles in migratory responses, adhesive signalling and mechanotransduction. FAK-dependent regulation of cell migration involves focal adhesion turnover dynamics as well as actin cytoskeleton polymerization and lamellipodia protrusion.
Whereas roles for FAK in migratory and mechanosensing responses have been established, the contribution of FAK to the generation of adhesive forces is not well understood.
Results. Using FAK-null cells expressing wild-type and mutant FAK under an inducible tetracycline promoter, we analysed the role of FAK in the generation of steady-state adhesive forces using micropatterned substrates and a hydrodynamic adhesion assay. FAK expression reduced steady-state strength by 30% compared with FAK-null cells.
FAK expression reduced VCL (vinculin) localization to focal adhesions by 35% independently of changes in integrin binding and localization of talin and paxillin. RNAi (RNA interference) knock-down of VCL abrogated the FAK-dependent differences in adhesive forces. FAK-dependent changes in VCL localization and adhesive forces were confirmed in human primary fibroblasts with FAK knocked down by RNAi. The autophosphorylation Tyr-397 and kinase domain Tyr-576/Tyr-577 sites were differentially required for FAK-mediated adhesive responses.
Conclusions. We demonstrate that FAK reduces steady-state adhesion strength by modulating VCL recruitment to focal adhesions. These findings provide insights into the role of FAK in mechanical interactions between a cell and

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