Fig. 4.
Fig. 4. Gab2 associates with the SHP-2 and SHP-1 phosphatases and the p85 subunit of PI3 kinase in the β1-integrin signaling pathway. / (A) Ba/F3 cells were stimulated by β1-integrin cross-linking for 5 and 15 minutes as indicated in the text. Cell lysates were prepared and anti-Gab2 immunoprecipitation was performed. Immunoprecipitates were resolved by SDS-PAGE and then blotted with anti-SHP-2, anti-p85 subunit of PI3 kinase, and anti-Gab2 Abs. (B) Anti-SHP-1 immunoprecipitation was conducted followed by anti-Gab2 Western blotting. (C) Cell lysates (500 μg) of Ba/F3 cells stimulated by β1-integrin cross-linking were incubated with 10 μg of the SHP-1 N- or C-terminal SH2 domain GST fusion proteins that were immobilized on glutathione beads for 4 hours. Bound proteins were resolved by SDS-PAGE and then immunoblotted with anti-Gab2 Ab. Shown are representatives of 2 independent experiments.

Gab2 associates with the SHP-2 and SHP-1 phosphatases and the p85 subunit of PI3 kinase in the β1-integrin signaling pathway.

(A) Ba/F3 cells were stimulated by β1-integrin cross-linking for 5 and 15 minutes as indicated in the text. Cell lysates were prepared and anti-Gab2 immunoprecipitation was performed. Immunoprecipitates were resolved by SDS-PAGE and then blotted with anti-SHP-2, anti-p85 subunit of PI3 kinase, and anti-Gab2 Abs. (B) Anti-SHP-1 immunoprecipitation was conducted followed by anti-Gab2 Western blotting. (C) Cell lysates (500 μg) of Ba/F3 cells stimulated by β1-integrin cross-linking were incubated with 10 μg of the SHP-1 N- or C-terminal SH2 domain GST fusion proteins that were immobilized on glutathione beads for 4 hours. Bound proteins were resolved by SDS-PAGE and then immunoblotted with anti-Gab2 Ab. Shown are representatives of 2 independent experiments.

Close Modal

or Create an Account

Close Modal
Close Modal