Beta integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation.

@article{Anthis2009BetaIT,
  title={Beta integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation.},
  author={Nicholas J. Anthis and Jacob R. Haling and Camilla L Oxley and Massimiliano Memo and Kate L Wegener and Chinten James Lim and Mark H Ginsberg and Iain D. Campbell},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 52},
  pages={36700-10}
}
Integrins are large membrane-spanning receptors fundamental to cell adhesion and migration. Integrin adhesiveness for the extracellular matrix is activated by the cytoskeletal protein talin via direct binding of its phosphotyrosine-binding-like F3 domain to the cytoplasmic tail of the beta integrin subunit. The phosphotyrosine-binding domain of the signaling protein Dok1, on the other hand, has an inactivating effect on integrins, a phenomenon that is modulated by integrin tyrosine… CONTINUE READING

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