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Related Experiment Videos

SHIPs ahoy.

G Krystal1, J E Damen, C D Helgason

  • 1Terry Fox Laboratory, BC Cancer Agency, Vancouver, Canada. gerryk@terryfox.ubc.ca

The International Journal of Biochemistry & Cell Biology
|December 3, 1999
PubMed
Summary
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Two related enzymes, SHIP and SHIP2, break down a key signaling molecule, phosphatidylinositol-3,4,5-trisphosphate. This action regulates cell functions like proliferation and prevents mast cell degranulation.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Two enzymes, src homology 2-containing inositol 5'-phosphatase (SHIP) and SHIP2, have been identified.
  • SHIP is specific to hemopoietic cells, while SHIP2 is more widely expressed.
  • Both enzymes hydrolyze phosphatidylinositol-3,4,5-trisphosphate (PIP3) and inositol 1,3,4,5-tetrakisphosphate in vitro.

Purpose of the Study:

  • To investigate the role of SHIP and SHIP2 in cellular signaling pathways.
  • To understand the enzymatic activity of SHIP and SHIP2 in hydrolyzing specific phosphoinositides.
  • To explore the potential of SHIPs in regulating various cellular processes.

Main Methods:

  • Independent cloning of SHIP and SHIP2 by three research groups.
  • In vitro enzymatic assays to determine substrate specificity.

Related Experiment Videos

  • In vivo studies in mast cells to elucidate SHIP's function in degranulation.

    • Main Results:

    • SHIP is the primary enzyme in normal mast cells responsible for degrading PIP3 into phosphatidylinositol-3,4-bisphosphate.
    • This enzymatic activity of SHIP limits normal mast cell degranulation and prevents inappropriate degranulation.
    • SHIP and SHIP2 demonstrate the ability to hydrolyze specific phosphoinositide substrates.

    Conclusions:

    • SHIP plays a crucial role in regulating mast cell degranulation.
    • SHIPs have the potential to modulate numerous phosphatidylinositol-3-kinase (PI3K)-induced cellular events.
    • Further research into SHIP and SHIP2 is warranted due to their regulatory roles in cell signaling.