Regulation of protein-tyrosine phosphatases alpha and epsilon by calpain-mediated proteolytic cleavage.

@article{GilHenn2001RegulationOP,
  title={Regulation of protein-tyrosine phosphatases alpha and epsilon by calpain-mediated proteolytic cleavage.},
  author={Hava Gil-Henn and Gloria Volohonsky and Ari Elson},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 34},
  pages={31772-9}
}
The precise subcellular localization of non-receptor tyrosine phosphatases is a major factor in regulating their physiological functions. We have previously shown that cellular processing of protein-tyrosine phosphatase epsilon (PTP epsilon) generates a physiologically distinct, cytoplasmic form of this protein, p65 PTP epsilon. Here we describe a novel protein form of the related receptor-type tyrosine phosphatase alpha (RPTP alpha), p66 PTP alpha, which is detected in nearly all cell types… CONTINUE READING

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