Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes

@article{Zachary1992FocalAK,
  title={Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes},
  author={Ian Zachary and Enrique Rozengurt},
  journal={Cell},
  year={1992},
  volume={71},
  pages={891-894}
}
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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.
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.
Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly
TLDR
A role for integrin- mediated tyrosine phosphorylation in the organization of the cytoskeleton as cells adhere to the extracellular matrix is suggested.
Bradykinin and bombesin rapidly stimulate tyrosine phosphorylation of a 120-kDa group of proteins in Swiss 3T3 cells.
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It is shown that an increase in tyrosine phosphorylation of a 120-kDa group of proteins is an early protein kinase C-independent cellular signal elicited by both bradykinin and bombesin.
Paxillin is a major phosphotyrosine-containing protein during embryonic development
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    The Journal of cell biology
  • 1991
TLDR
The data suggest that the regulated phosphorylation of tyrosine residues on paxillin may perform a critical role in controlling cell and tissue cytoarchitecture rearrangement during vertebrate development.