The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation.

@article{Zhang2003TheRO,
  title={The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation.},
  author={Zhongsen Zhang and Kui Shen and Wei Lu and Philip A Cole},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 7},
  pages={
          4668-74
        }
}
The protein-tyrosine phosphatase SHP-1 plays a variety of roles in the "negative" regulation of cell signaling. The molecular basis for the regulation of SHP-1 is incompletely understood. Whereas SHP-1 has previously been shown to be phosphorylated on two tail tyrosine residues (Tyr(536) and Tyr(564)) by several protein-tyrosine kinases, the effects of these phosphorylation events have been difficult to address because of the intrinsic instability of the linkages within a protein-tyrosine… CONTINUE READING

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