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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