Identification of p125, a component of a group of 120-kDa proteins that are phosphorylated on tyrosine residues in response to bradykinin and bombesin stimulation, in anti-ras-GTPase-activating protein immunoprecipitates of Swiss 3T3 cells.

@article{LeebLundberg1993IdentificationOP,
  title={Identification of p125, a component of a group of 120-kDa proteins that are phosphorylated on tyrosine residues in response to bradykinin and bombesin stimulation, in anti-ras-GTPase-activating protein immunoprecipitates of Swiss 3T3 cells.},
  author={L. M. Leeb-Lundberg and X. Song},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 11},
  pages={
          8151-7
        }
}
Bradykinin (BK) and bombesin (BN) stimulate an increase in the tyrosine phosphorylation of a 120-kDa group of proteins (pps120) in Swiss 3T3 cells (Leeb-Lundberg, L. M. F., and Song X.-H. (1991) J. Biol. Chem. 266, 7746-7749). Here, we show that a component of pps120, p125, was specifically immunoprecipitated with antibodies against the p21ras GTPase-activating protein (GAP). The major portion of GAP in nonstimulated cells (96%) was located in the cytosol, and this distribution was not affected… Expand
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