PTP1B modulates the association of beta-catenin with N-cadherin through binding to an adjacent and partially overlapping target site.

@article{Xu2002PTP1BMT,
  title={PTP1B modulates the association of beta-catenin with N-cadherin through binding to an adjacent and partially overlapping target site.},
  author={Gang Xu and Carlos O. Arregui and Jack E. Lilien and J. Whitney Balsamo},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 51},
  pages={
          49989-97
        }
}
The nonreceptor tyrosine phosphatase PTP1B associates with the cytoplasmic domain of N-cadherin and may regulate cadherin function through dephosphorylation of beta-catenin. We have now identified the domain on N-cadherin to which PTP1B binds and characterized the effect of perturbing this domain on cadherin function. Deletion constructs lacking amino acids 872-891 fail to bind PTP1B. This domain partially overlaps with the beta-catenin binding domain. To further define the relationship of… CONTINUE READING
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