Fig. 4. ß3 integrin mediates autophosphorylation of FAK and the activity of Src. The cells were plated on VN without serum for 30 minutes on all panels. (A) Cells were extracted and immunoprecipitated with anti-FAK antibodies followed by western blotting with anti-pTyr³⁹⁷ antibodies (top). The membrane was stripped and reprobed with anti-FAK antibodies (bottom). (B) The cell lysates were immunoprecipitated with anti-Src antibodies. The immune complexes were analyzed for the incorporation of -³²P by kinase assay (top). To ensure equivalent amounts of immunoprecipitated protein, the lysates were immunoprecipitated followed by western blotting with anti-Src antibodies (bottom). Autophosphorylation of Fyn was analyzed by kinase assay (top). The relative amount of immunoprecipitated protein was analyzed by an immunoprecipitation followed by western blotting with anti-Fyn antibodies (bottom). (C) To detect putative complex formation, samples were immunoprecipitated with anti-Src antibodies followed by western blotting with antibodies to FAK (top). Relative amounts of immunoprecipitated protein were determined by an immunoprecipitation followed by western blotting with anti-Src antibodies (bottom). To detect FAK/Fyn complex formation, samples were immunoprecipitated with anti-FAK antibodies followed by western blotting with anti-Fyn antibodies (top). Relative amounts of Fyn were identified by immunoprecipitation followed by western blotting with anti-Fyn antibodies (bottom).

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