Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation

@article{Guan1992RegulationOF,
  title={Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation},
  author={Jun-Lin Guan and David Shalloway},
  journal={Nature},
  year={1992},
  volume={358},
  pages={690-692}
}
INCREASING evidence indicates that the integrin family of cell adhesion receptors can transduce biochemical signals from the extracellular matrix to the cell interior to modulate cell growth and differentiation1. We have shown that integrin/ligand interactions can trigger tyrosine phosphorylation of a protein of Mr 120,000 (pp120), so it is possible that signal transduction by integrins might involve activation of intracellular protein tyrosine kinases as an early event in cell binding to the… 
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References

SHOWING 1-10 OF 14 REFERENCES
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.
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.
pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.
TLDR
The isolation of a cDNA encoding a protein, pp125, that is a major phosphotyrosine-containing protein in untransformed chicken embryo cells and exhibits an increase in phosphotYrosine in pp60v-src-transformedChicken embryo cells is reported.
Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases.
TLDR
Monoclonal antibodies are generated to detect several of the same tyrosine phosphoproteins in chicken embryo fibroblasts transformed by avian retroviruses Y73 and CT10, encoding the yes and crk oncogenes, respectively.
Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton
TLDR
A new approach to both the identification of membrane skeletal proteins in fibroblasts and changes that occur upon transformation by an activated tyrosine kinase is offered.
A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants.
TLDR
In Xenopus oocytes, this protein maintains normal p21 in a biologically inactive, GDP-bound state through its effect on GTPase activity, and it appears that the major effect of position 12 mutations is to prevent this protein from stimulating p21 GTP enzyme activity, thereby allowing these mutants to remain in the active GTP- bound state.
Interaction of serum and cell spreading affects the growth of neoplastic and non-neoplastic fibroblasts.
TLDR
It is found that more spreading increased net growth of both neoplastic and non-neoplastic cells, while less spreading depressed growth, and it appears that the sensitivity of cells to humoral factors is governed by cell spreading.
Isolation of antibodies for phosphotyrosine by immunization with a v-abl oncogene-encoded protein.
  • J. Wang
  • Biology
    Molecular and cellular biology
  • 1985
TLDR
The usefulness of these antibodies was demonstrated by the detection of previously unidentified tyrosine-phosphorylated proteins in v-src, v-abl-, and v-erbB-transformed cell lines.
...
1
2
...