• Corpus ID: 3019735

Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn.

@article{Cary1996StimulationOC,
  title={Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn.},
  author={Leslie A. Cary and J F Chang and Jun-Lin Guan},
  journal={Journal of cell science},
  year={1996},
  volume={109 ( Pt 7)},
  pages={
          1787-94
        }
}
Cellular interactions with the extracellular matrix proteins play important roles in a variety of biological processes. Recent studies suggest that integrin-mediated cell-matrix interaction can transduce biochemical signals across the plasma membrane to regulate cellular functions such as proliferation, differentiation and migration. These studies have implicated a critical role of focal adhesion kinase (FAK) in integrin-mediated signal transduction pathways. We report here that overexpression… 
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Identification of p130Cas as a Mediator of Focal Adhesion Kinase–promoted Cell Migration
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P130Cas, but not Grb2, is a mediator of FAK-promoted cell migration and it is suggested that FAK/ p130Cas complex targets downstream pathways other than Erks in mediatingFAK- Promoted Cell migration.
Focal adhesion kinase and its signaling pathways in cell migration and angiogenesis.
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Focal adhesion kinase (FAK) was first described in 1992 as a novel nonreceptor protein-tyrosine kinase localized prominently within focal adhesions, suggesting a signaling role in regulating cell…
Regulation of focal adhesion kinase by a novel protein inhibitor FIP200.
TLDR
Results identify FIP200 as a novel protein inhibitor for FAK, which is decreased upon integrin-mediated cell adhesion concomitant with FAK activation and leads to increased FAK phosphorylation and partial restoration of cell cycle progression in cells plated on poly-L-lysine, providing further support for FIP 200 as a negative regulator of FAK.
Association of Focal Adhesion Kinase with Grb7 and Its Role in Cell Migration*
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It is reported that the SH2 domain of Grb7 can directly interact with FAK through Tyr-397, a major autophosphorylation site in vitro and in vivo, suggesting that the FAK-Grb7 complex is involved in integrin signaling.
Analysis of FAK‐associated signaling pathways in the regulation of cell cycle progression
Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration.
TLDR
It is shown that stable re-expression of epitope-tagged FAK reversed the morphological defects of the FAK- cells through the dynamic regulation of actin structures and focal contact sites in fibronectin (FN) stimulated cells.
Signal transduction by focal adhesion kinase in cancer
TLDR
The intensive research on FAK signaling in cancer have yielded a wealth of information on this pivotal kinase and these and future studies are leading to potentially novel therapies for cancer.
Role of focal adhesion kinase in integrin signaling.
  • J. Guan
  • Biology, Chemistry
    The international journal of biochemistry & cell biology
  • 1997
Focal adhesion kinase in cancer
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The biology of FAK is reviewed to determine whether FAK inhibition might provide the much needed ‘magic bullet’ in cancer therapeutics.
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References

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The interaction of cells with extracellular matrix proteins plays a critical role in a variety of biological processes. Recent studies suggest that cell-matrix interactions mediated by integrins can…
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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
The stable association of FAK with phosphatidylinositol 3-kinase in NIH 3T3 mouse fibroblasts and direct phosphorylation of p85 by FAK in vitro suggest that PI 3-Kinase may be a FAK substrate in vivo and serve as an effector of FAk.
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TLDR
FAK may mediate signal transduction events initiated on the cell surface by kinase activation and autophosphorylation that result in its binding to other key intracellular signaling molecules.
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TLDR
It is shown that tyrosineosphorylation of this protein is modulated both by cell adhesion and transformation by pp60v–src, and that these changes in phosphorylation are correlated with increased pp125FAKtyrosine kinase activity.
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TLDR
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TLDR
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TLDR
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TLDR
It is postulated that the integrin-stimulated tyrosine phosphorylation of pp130 may reflect part of an important signal transduction process between the extracellular matrix and the cell interior.
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TLDR
A role for integrin- mediated tyrosine phosphorylation in the organization of the cytoskeleton as cells adhere to the extracellular matrix is suggested.
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TLDR
The entire mouse FadK amino acid sequence was deduced from cDNA clones, revealing a large non-membrane-spanning protein-tyrosine kinase that lacks Src-homology SH2 and SH3 domains.
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