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…
614 Citations
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References
SHOWING 1-10 OF 58 REFERENCES
Interaction of Focal Adhesion Kinase with Cytoskeletal Protein Talin (*)
- BiologyThe Journal of Biological Chemistry
- 1995
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…
Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1994
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.
Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain.
- Biology, ChemistryMolecular biology of the cell
- 1994
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.
Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
- BiologyNature
- 1992
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.
Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
- BiologyNature
- 1995
Surprisingly, the number of focal adhesions was increased in FAK-deficient cells, suggesting that FAK may be involved in the turnover of focalAdhesion contacts during cell migration.
Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
- Biology, ChemistryNature
- 1994
It is shown that adhesion of murine NIH3T3 fibroblasts to fibronectin promotes SH2-domain-mediated association of the GRB2 adaptor protein and the c-Src protein-tyrosine kinase (PTK) with FAK in vivo, and also results in activation of mitogen-activated protein Kinase (MAPK).
Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions
- BiologyThe Journal of cell biology
- 1993
An analysis of the domain structure of FAK is reported in which a contiguous stretch of 159 amino acids within the COOH terminus essential for correct subcellular localization is identified, suggesting that pp125FAK cannot be activated oncogenically by mutation.
Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1991
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.
Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly
- BiologyThe Journal of cell biology
- 1992
A role for integrin- mediated tyrosine phosphorylation in the organization of the cytoskeleton as cells adhere to the extracellular matrix is suggested.
Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1992
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.