Alternative splicing controls the mechanisms of FAK autophosphorylation.

@article{Toutant2002AlternativeSC,
  title={Alternative splicing controls the mechanisms of FAK autophosphorylation.},
  author={Madeleine Toutant and Alicia Costa and Jeanne-Marie Studler and Gress Kadar{\'e} and Mich{\`e}le Carnaud and Jean-Antoine Girault},
  journal={Molecular and cellular biology},
  year={2002},
  volume={22 22},
  pages={7731-43}
}
Focal adhesion kinase (FAK) is activated following integrin engagement or stimulation of transmembrane receptors. Autophosphorylation of FAK on Tyr-397 is a critical event, allowing binding of Src family kinases and activation of signal transduction pathways. Tissue-specific alternative splicing generates several isoforms of FAK with different autophosphorylation rates. Despite its importance, the mechanisms of FAK autophosphorylation and the basis for differences between isoforms are not known… CONTINUE READING
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