Autophosphorylation of Tyr397 and its phosphorylation by Src-family kinases are altered in focal-adhesion-kinase neuronal isoforms.

@article{Toutant2000AutophosphorylationOT,
  title={Autophosphorylation of Tyr397 and its phosphorylation by Src-family kinases are altered in focal-adhesion-kinase neuronal isoforms.},
  author={Madeleine Toutant and J. M. Studler and Ferr{\'a}n Burgaya and Alicia Costa and Pascal Ezan and Marina S. Gelman and Jean Antoine Girault},
  journal={The Biochemical journal},
  year={2000},
  volume={348 Pt 1},
  pages={119-28}
}
In brain, focal adhesion kinase (FAK) is regulated by neurotransmitters and has a higher molecular mass than in other tissues, due to alternative splicing. Two exons code for additional peptides of six and seven residues ('boxes' 6 and 7), located on either side of Tyr(397), which increase its autophosphorylation. Using in situ hybridization and a monoclonal antibody (Mab77) which does not recognize FAK containing box 7, we show that, although mRNAs coding for boxes 6 and 7 have different… CONTINUE READING

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