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Related Experiment Videos

Sap-1/PTPRH activity is regulated by reversible dimerization.

Sébastien Wälchli1, Xavier Espanel, Rob Hooft van Huijsduijnen

  • 1Serono Pharmaceutical Research Institute, 14, chemin des Aulx, Plan-les-Ouates/Geneva, Switzerland.

Biochemical and Biophysical Research Communications
|April 27, 2005
PubMed
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Sap-1/PTPRH, a receptor protein tyrosine phosphatase, forms stable homodimers via its extracellular and transmembrane domains. This dimerization regulates its catalytic activity and interaction with c-src, a novel substrate.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Sap-1/PTPRH (protein tyrosine phosphatase receptor type H) is ubiquitously expressed and upregulated in gastrointestinal cancers.
  • Receptor protein tyrosine phosphatases (RPTPs) play critical roles in cellular signaling and are implicated in various diseases.

Purpose of the Study:

  • To investigate the oligomeric state and dimerization mechanism of Sap-1/PTPRH.
  • To identify the domains responsible for Sap-1 dimerization and its regulation.
  • To characterize the functional consequences of Sap-1 dimerization on its catalytic activity and substrate interactions.

Main Methods:

  • Chemical cross-linking and co-immunoprecipitation to assess Sap-1 oligomerization.
  • Analysis of Sap-1 domains involved in dimerization.

Related Experiment Videos

  • Assessment of Sap-1 catalytic activity in dimer and monomer states.
  • Identification of c-src as a novel Sap-1 substrate.

    • Main Results:

    • Overexpressed full-length Sap-1 forms stable homodimers.
    • Dimerization is mediated by the extracellular and transmembrane domains, not the catalytic domain.
    • Disruption of dimers by reducing agents suggests a role for cysteine bonds.
    • Sap-1 dimerization regulates its catalytic activity, with monomers exhibiting higher activity.
    • c-src is identified as a novel substrate dephosphorylated and activated by Sap-1.

    Conclusions:

    • Sap-1/PTPRH exists as a regulated homodimer, with dimerization mediated by its non-catalytic domains.
    • Cysteine bonds likely stabilize the Sap-1 dimer.
    • The dimer-monomer equilibrium influences Sap-1's phosphatase activity.
    • Sap-1 regulates c-src activity, suggesting a role in cancer signaling pathways.