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CIN85 interacting proteins in B cells-specific role for SHIP-1

Tom Büchse1, Nikolaus Horras, Eva Lenfert

  • 1Institute of Medical Biochemistry and Molecular Biology, Medical Faculty, University of Rostock, Schillingallee 70, 18057 Rostock, Germany. tom.buechse@med.uni-rostock.de

Molecular & Cellular Proteomics : MCP
|July 5, 2011
PubMed

Insights

Cbl-interacting protein 85 (CIN85) regulates receptor tyrosine kinase signaling in B lymphocytes. CIN85 interacts with SHIP-1, potentially enhancing the down-regulation of phosphatidylinositol-3,4,5-trisphosphate levels.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Cbl-interacting protein 85 (CIN85) is a key adaptor protein regulating receptor tyrosine kinase (RTK) signaling.
  • CIN85 enhances RTK-activated endocytosis and reduces phosphatidylinositol-3-kinase (PI3K)-induced phosphatidylinositol-3,4,5-trisphosphate (PIP3) production.
  • CIN85 expression is reported in primary splenic B lymphocytes and B-lymphoma cell lines.

Purpose of the Study:

  • To investigate the role and interactions of CIN85 in B lymphocytes.
  • To identify novel CIN85-interacting proteins in B cells.
  • To elucidate the functional significance of CIN85-SHIP-1 interaction in B cell signaling.

Main Methods:

  • Western blotting and co-immunoprecipitation to study protein associations.
  • Pull-down proteomics to identify CIN85 interactors.
  • Analysis of CIN85 and SHIP-1 interaction domains.

Main Results:

  • Cross-linking of the B cell antigen receptor increased CIN85 association with Cbl.
  • Proteomics identified 51 CIN85-interacting proteins in B cells, including novel partners.
  • SH2-containing inositol phosphatase 1 (SHIP-1) constitutively co-precipitated with CIN85 via its SH3 domains and a specific C-terminal region.

Conclusions:

  • CIN85 is expressed in B lymphocytes and interacts with Cbl upon B cell receptor stimulation.
  • A novel interaction between CIN85 and SHIP-1 was identified in B cells.
  • The CIN85-SHIP-1 interaction may synergistically down-regulate PI3K/PIP3 signaling in lymphocytes.

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