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ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex regulates MAP kinase signaling in human cancers

Paola D Vermeer1, Megan Bell, Kimberly Lee

  • 1Cancer Biology Research Center, Sanford Research/University of South Dakota, Sioux Falls, South Dakota, United States of America.

Plos One
|January 27, 2012
PubMed

Insights

Protein tyrosine phosphatase PTPN13 acts as a tumor suppressor in breast cancer by regulating the ErbB2, Src, and EphrinB1 signaling complex. Its reduced function enhances cancer signaling, suggesting EphrinB1 as a therapeutic target.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Oncology

Background:

  • Phosphatases regulate transient protein phosphorylation and signaling pathways.
  • Compromised phosphatase activity is linked to cancer development.
  • PTPN13, a non-receptor phosphatase, is a putative tumor suppressor with decreased expression in breast cancer, correlating with poor survival.

Purpose of the Study:

  • To investigate the role of PTPN13 in regulating signaling complexes in breast cancer.
  • To identify novel interactions and pathways involving PTPN13 in breast cancer.

Main Methods:

  • Co-immunoprecipitation assays to detect protein interactions.
  • Localization studies to determine protein location within cells.
  • Analysis of signaling pathway activation (e.g., MAP Kinase).

Main Results:

  • PTPN13 regulates a novel signaling complex involving ErbB2, Src, and EphrinB1 in breast cancer.
  • EphrinB1, a PTPN13 substrate, interacts with ErbB2, an interaction enhanced by the V660E ErbB2 mutation.
  • Src kinase phosphorylates EphrinB1, activating MAP Kinase signaling, which is further enhanced by decreased PTPN13 function.

Conclusions:

  • The identified signaling complex highlights a new mechanism in breast cancer.
  • EphrinB1 may represent a therapeutic target in breast cancers with ErbB2 mutations and reduced PTPN13 expression.

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