The transmembrane protein tyrosine phosphatase alpha dephosphorylates the insulin receptor in intact cells.

@article{Lammers1997TheTP,
  title={The transmembrane protein tyrosine phosphatase alpha dephosphorylates the insulin receptor in intact cells.},
  author={Reiner Lammers and N P M\ołler and Axel Ullrich},
  journal={FEBS letters},
  year={1997},
  volume={404 1},
  pages={37-40}
}
Protein tyrosine phosphatases (PTPs) are key regulators in a variety of signal transduction processes. However, substrates for most PTPs have not been determined. In a previous report, we demonstrated that in a transient expression system the intracellular phosphatases PTPs 1B and TC preferentially dephosphorylated the precursor form of several receptor tyrosine kinases. In this paper we show that the dephosphorylation of kinase precursors is a specific feature of PTPs 1B and TC that is not… CONTINUE READING