Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.

@article{Panetti2002TyrosinePO,
  title={Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.},
  author={Tracee Scalise Panetti},
  journal={Frontiers in bioscience : a journal and virtual library},
  year={2002},
  volume={7},
  pages={
          d143-50
        }
}
  • T. S. Panetti
  • Published 2002
  • Biology
  • Frontiers in bioscience : a journal and virtual library
Integrins are transmembrane receptors that mediate cell attachment to the substrate. At the cytoplasmic surface of the integrin, cytoskeletal proteins cluster into focal adhesions. The focal adhesions contain multiple proteins that provide a structural and signaling complex inside the cell. This review focuses on three of the cytoskeletal components of the focal adhesion, paxillin, FAK, and p130CAS, that are phosphorylated and play a regulatory role in cell spreading and cell migration. A brief… 
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TLDR
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Characterization of the Phospho-Adhesome by Mass Spectrometry-Based Proteomics.
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Compared to phosphoproteomic analyses of cell lysates, the workflow described here enables an improved detection of phosphorylation sites from well-defined IAC proteins, including many known components of the signaling pathways activated by adhesion to the ECM.
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