Src homology 2 domains of protein tyrosine phosphatase are phosphorylated by insulin receptor kinase and bind to the COOH-terminus of insulin receptors in vitro.

@article{Maegawa1993SrcH2,
  title={Src homology 2 domains of protein tyrosine phosphatase are phosphorylated by insulin receptor kinase and bind to the COOH-terminus of insulin receptors in vitro.},
  author={Hiroshi Maegawa and Satoshi Ugi and Osamu Ishibashi and R Tachikawa-Ide and Noriko Takahara and Yasushi Tanaka and Yukiko Takagi and Ryuichi Kikkawa and Yukio Shigeta and Atsunori Kashiwagi},
  journal={Biochemical and biophysical research communications},
  year={1993},
  volume={194 1},
  pages={208-14}
}
To clarify the role of protein tyrosine phosphatases(PTPase) containing Src homology 2 (SH2) regions on insulin signaling, we investigated the interactions between SH2 regions of PTPase and insulin receptors. We made a pair of SH2 domains of PTP1C and SH-PTP2 fusion proteins coupled to glutathione-S-transferase (GST) using pGEX-3X expression vector. After incubating with insulin, insulin receptors were incubated with SH2 proteins in the presence of 100 mu ATP at 4 degrees C for 3 hr, and then… CONTINUE READING