Tyrosine phosphorylation of the beta 4 integrin cytoplasmic domain mediates Shc signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes.

@article{Dans2001TyrosinePO,
  title={Tyrosine phosphorylation of the beta 4 integrin cytoplasmic domain mediates Shc signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes.},
  author={Michael J Dans and Laurent Gagnoux-Palacios and Pamela Blaikie and Stephanie Z Klein and Agnese Mariotti and Filippo G. Giancotti},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 2},
  pages={1494-502}
}
Ligation of the alpha(6)beta(4) integrin induces tyrosine phosphorylation of the beta(4) cytoplasmic domain, followed by recruitment of the adaptor protein Shc and activation of mitogen-activated protein kinase cascades. We have used Far Western analysis and phosphopeptide competition assays to map the sites in the cytoplasmic domain of beta(4) that are required for interaction with Shc. Our results indicate that, upon phosphorylation, Tyr(1440), or secondarily Tyr(1422), interacts with the SH2… CONTINUE READING

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