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Focal adhesion kinase: the first ten years

Journal of Cell Science · 2003 · Vol. 116(8) · pp. 1409–1416
J. Thomas Parsons

Abstract

The protein tyrosine kinase focal adhesion kinase (FAK) plays a prominent role in integrin signaling. FAK activation, demonstrated by an increase in phosphorylation of Tyr397 as well as other sites in the protein, is best understood in the context of the engagement of integrins at the cell surface. Activation of FAK results in recruitment of a number of SH2-domain- and SH3-domain-containing proteins, which mediate signaling to several downstream pathways. FAK-dependent activation of these pathways has been implicated in a diverse array of cellular processes, including cell migration, growth factor signaling, cell cycle progression and cell survival.

Cell Adhesion Molecules ResearchCellular Mechanics and InteractionsProtein Kinase Regulation and GTPase SignalingFocal adhesionBiologyCell biologyPTK2IntegrinSignal transductionCell adhesionTyrosine kinaseContext (archaeology)SH2 domain

MeSH terms

AnimalsCell MovementCell SurvivalCytoskeletal ProteinsHumansModels, BiologicalProtein-Tyrosine KinasesSignal TransductionIntegrinsFocal AdhesionsFocal Adhesion Protein-Tyrosine KinasesFocal Adhesion Kinase 1

Funding

  • National Institutes of Health
  • National Cancer Institute
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