The association of focal adhesion kinase with a 200-kDa protein that is tyrosine phosphorylated in response to platelet-derived growth factor.

@article{Chen1996TheAO,
  title={The association of focal adhesion kinase with a 200-kDa protein that is tyrosine phosphorylated in response to platelet-derived growth factor.},
  author={H. C. Chen and Jun-Lin Guan},
  journal={European journal of biochemistry},
  year={1996},
  volume={235 3},
  pages={
          495-500
        }
}
Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase implicated in the signal transduction pathways initiated by integrins. However, we have previously found that platelet-derived growth factor (PDGF) could stimulate the association of FAK with phosphatidylinositol 3-kinase in NIH 3T3 cells [Chen, H.-C. & Guan, J.-L. (1994) J. Biol. Chem 269, 31229-31223], suggesting that FAK might participate in some of the cellular effects of the growth factors in modulating cell morphology and… 
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References

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Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase.
  • H. C. Chen, J. Guan
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1994
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.
Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
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.
Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin.
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.
Internalization of activated platelet-derived growth factor receptor-phosphatidylinositol-3' kinase complexes: potential interactions with the microtubule cytoskeleton.
TLDR
The results suggest that PDGF receptor-p85 complexes internalize and transit in association with the microtubule cytoskeleton, and the high concentration of p85 in intracellular structures in the absence of PDGF stimulation suggests additional roles for this protein independent of its association with receptor tyrosine kinases.
Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.
TLDR
Interaction of beta 1 integrins with extracellular ligands (fibronectin or antibodies) triggers phosphorylation of an intracellular 120-kDa protein, pp120, that may be involved in the responses of cells to attachment.
Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins.
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.
Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
TLDR
This study provides the first genetic evidence that tyrosine phosphorylation of pp125FAK is dependent on integrin- mediated events, and demonstrates that there is a strong correlation between tyrosines phosphorylated in platelets, and the activation of pp 125FAK-associated phosphorylating activity in vitro.
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