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FOCAL ADHESIONS, CONTRACTILITY, AND SIGNALING
Author(s) -
Keith Burridge,
Magdalena ChrzanowskaWodnicka
Publication year - 1996
Publication title -
annual review of cell and developmental biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 11.094
H-Index - 220
eISSN - 1530-8995
pISSN - 1081-0706
DOI - 10.1146/annurev.cellbio.12.1.463
Subject(s) - focal adhesion , microbiology and biotechnology , extracellular matrix , ptk2 , integrin , biology , signal transduction , actin cytoskeleton , cytoskeleton , actin , fibronectin , extracellular , receptor , cell , protein kinase c , biochemistry , mitogen activated protein kinase kinase
Focal adhesions are sites of tight adhesion to the underlying extracellular matrix developed by cells in culture. They provided a structural link between the actin cytoskeleton and the extracellular matrix and are regions of signal transduction that relate to growth control. The assembly of focal adhesions is regulated by the GTP-binding protein Rho. Rho stimulates contractility which, in cells that are tightly adherent to the substrate, generates isometric tension. In turn, this leads to the bundling of actin filaments and the aggregation of integrins (extracellular matrix receptors) in the plane of the membrane. The aggregation of integrins activates the focal adhesion kinase and leads to the assembly of a multicomponent signaling complex.

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