Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC.

@article{Hower2009DimerizationOT,
  title={Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC.},
  author={Amy E Hower and Pedro J. Beltran and John L. Bixby},
  journal={Journal of neurochemistry},
  year={2009},
  volume={110 5},
  pages={1635-47}
}
Receptor-protein tyrosine phosphatases (RPTPs), like receptor tyrosine kinases, regulate neuronal differentiation. While receptor tyrosine kinases are dimerized and activated by extracellular ligands, the extent to which RPTPs dimerize, and the effects of dimerization on phosphatase activity, are poorly understood. We have examined a neuronal type III RPTP, PTPRO; we find that PTPRO can form dimers in living cells, and that disulfide linkages in PTPROs intracellular domain likely regulate… CONTINUE READING

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