The low M r phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase

@article{Bucciantini1999TheLM,
  title={The low M
r phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase},
  author={M. Bucciantini and P. Chiarugi and P. Cirri and L. Taddei and M. Stefani and G. Raugei and P. Nordlund and G. Ramponi},
  journal={FEBS Letters},
  year={1999},
  volume={456}
}
The low molecular weight phosphotyrosine protein phosphatase (LMW‐PTP) is phosphorylated by Src and Src‐related kinases both in vitro and in vivo; in Jurkat cells, and in NIH‐3T3 cells, it becomes tyrosine‐phosphorylated upon stimulation by PDGF. In this study we show that pp60Src phosphorylates in vitro the enzyme at two tyrosine residues, Tyr131 and Tyr132, previously indicated as the main phosphorylation sites of the enzyme, whereas phosphorylation by the PDGF‐R kinase is much less effective… Expand
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