Science in China Series C: Life Sciences

, Volume 48, Issue 2, pp 163–167 | Cite as

Structural basis of interaction between protein tyrosine phosphatase PCP-2 and β-catenin

  • Yaqin He
  • Hexin Yan
  • Hui Dong
  • Peng Zhang
  • Liang Tang
  • Xiuhua Qiu
  • Mengchao Wu
  • Hongyang Wang
Article

Abstract

PCP-2 is a member of receptor-like protein tyrosine phosphatase of the MAM domain family. To investigate which part of PCP-2 was involved in its interaction with β-catenin, we constructed various deletion mutants of PCP-2. These PCP-2 mutants and wild-type PCP-2 were co-transfected into BHK-21 cells with β-catenin individually. Anin vivo binding assay revealed that the expression of wild-type PCP-2, PCP-2 ΔC1C2 (deleted PCP-2 without both PTP domains) and PCP-2 ΔC2 (deleted PCP-2 without the second PTP domain) could be immunoprecipitated by anti-catenin antibody in every co-transfection, but PCP-2 EXT (deleted PCP-2 without the juxtamembrane region and both PTP domains) was missing, which implied that PCP-2 and β-catenin could associate directly and the juxtamembrane region in PCP-2 was sufficient for the process.

Keywords

PCP-2 β-catenin protein tyrosine phosphatase interaction 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Cheng, A., Dube, N., Gu, F. et al., Coordinated action of protein tyrosine phosphatases in insulin signal transduction, Eur. J. Biochem., 2002, 269(4): 1050–1059.PubMedCrossRefGoogle Scholar
  2. 2.
    Sorenson, C. M., Sheibani, N., Altered regulation of SHP-2 and PTP 1B tyrosine phosphatases in cystic kidneys from bcl-2-/-mice, Am. J. Physiol. Renal Physiol., 2002, 282(3): F442–450.PubMedGoogle Scholar
  3. 3.
    Kennedy, B. P., Ramachandran, C., Protein tyrosine phosphatase-1B in diabetes, Biochem. Pharmacol., 2000, 60(7): 877–883.PubMedCrossRefGoogle Scholar
  4. 4.
    Uzui, H., Lee, J. D., Shimizu, H. et al., The role of protein-tyrosine phosphorylation and gelatinase production in the migration and proliferation of smooth muscle cells, Atherosclerosis, 2000, 149(1): 51–59.PubMedCrossRefGoogle Scholar
  5. 5.
    Wang, H., Lian, Z., Lerch, M. M. et al., Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family, Oncogene, 1996, 12(12): 2555–2562. main family, Oncogene, 1996, 12(12): 2555–2562.PubMedGoogle Scholar
  6. 6.
    Yan, H. X., He, Y. Q., Wu, M. C. et al., Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and β-catenin, Biochemistry, 2002, 41(52): 15854–15860.PubMedCrossRefGoogle Scholar
  7. 7.
    Chan, S. W., Hong, W., Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription, J. Biol. Chem., 2001, 276(30): 28402–28412.PubMedCrossRefGoogle Scholar
  8. 8.
    Ho, A. T., Voura, E. B., Soloway, P. D. et al., MMP inhibitors augment fibroblast adhesion through stabilization of focal adhesion contacts and up-regulation of cadherin function, J. Biol. Chem., 2001, 276(43): 40215–40224.PubMedGoogle Scholar
  9. 9.
    Marambaud, P., Shioi, J., Serban, G. et al., A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions, EMBO J., 2002, 21(8): 1948–1956.PubMedCrossRefGoogle Scholar
  10. 10.
    Fuchs, M., Muller, T., Lerch, M. M. et al., Association of human protein-tyrosine phosphatase kappa with members of the armadillo family, J. Biol. Chem., 1996, 271(28): 16712–16719.PubMedCrossRefGoogle Scholar
  11. 11.
    Tonks, N. K., Neel, B. G., Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding, Mol. Cell Biol., 1994, 14(1): 1–9.Google Scholar
  12. 12.
    Hu, P., O’Keefe, E. J., Rubenstein, D. S., Tyrosine phosphorylation of human keratinocyte beta-catenin and plakoglobin reversibly regulates their binding to E-cadherin and alpha-catenin, J. Invest. Dermatol., 2001, 117(5): 1059–1067.PubMedCrossRefGoogle Scholar

Copyright information

© Science in China Press 2005

Authors and Affiliations

  • Yaqin He
    • 1
  • Hexin Yan
    • 1
  • Hui Dong
    • 1
  • Peng Zhang
    • 1
  • Liang Tang
    • 1
  • Xiuhua Qiu
    • 1
  • Mengchao Wu
    • 1
  • Hongyang Wang
    • 1
  1. 1.International Co-operation Laboratory on Signal TransductionEastern Hepatobiliary Surgery Hospital, Second Military Medical UniversityShanghaiChina

Personalised recommendations