SH2 domains mediate the sequential phosphorylation of HS1 protein by p72syk and Src-related protein tyrosine kinases.

@article{Ruzzene1996SH2DM,
  title={SH2 domains mediate the sequential phosphorylation of HS1 protein by p72syk and Src-related protein tyrosine kinases.},
  author={Maria Ruzzene and Anna Maria Brunati and Oriano Marin and Arianna Donella-Deana and Lorenzo A Pinna},
  journal={Biochemistry},
  year={1996},
  volume={35 16},
  pages={5327-32}
}
The protein tyrosine kinase p72syk readily phosphorylates hematopoietic linkage cell-specific protein p50/HS1 with high stoichiometry (up to 4 mol of Pi/mol of protein) and favorable kinetic constants (Km 77 nM, kcat 0.37 s-1), at sites that display the motif that is specifically recognized by the HS2 domains of Src tyrosine kinases. Such a phosphorylation converts p50/HS1 into a good substrate for c-Fgr, which in contrast is nearly inactive on nonphosphorylated p50/HS1. A phosphopeptide… CONTINUE READING