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    Regulation of phosphatidylinositol 3,4,5-trisphosphate 5'-phosphatase activity by insulin

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    Authors
    Guilherme, Adilson L.
    Klarlund, Jes K.
    Krystal, Gerald
    Czech, Michael P.
    UMass Chan Affiliations
    Program in Molecular Medicine and Department of Biochemistry and Molecular Biology
    Document Type
    Journal Article
    Publication Date
    1996-11-22
    Keywords
    Animals
    CHO Cells
    Cricetinae
    Humans
    Insulin
    Phosphoric Monoester Hydrolases
    Phosphorylation
    Precipitin Tests
    Receptor, Insulin
    Recombinant Proteins
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    https://doi.org/10.1074/jbc.271.47.29533
    Abstract
    Polyphosphoinositides are thought to be mediators of cellular signaling pathways as well as regulators of cytoskeletal elements and membrane trafficking events. It has recently been demonstrated that a class of phosphatidylinositol (PI) 3,4,5-P3 5'-phosphatases contains SH2 domains and proline-rich regions, which are present in many signaling proteins. We report here that insulin stimulation of Chinese hamster ovary cells (CHO-T) expressing human insulin receptors causes an 8-10-fold increase in PI 3,4,5-P3 5'-phosphatase activity in anti-phosphotyrosine immunoprecipitates of the cell lysates. This insulin-sensitive polyphosphoinositide 5'-phosphatase did not catalyze dephosphorylation of PI 4,5-P2. No change in 5'-phosphatase activity was detected in insulin receptor or IRS-1 immune complexes in response to insulin. However, insulin treatment of CHO-T cells markedly increased the PI 3,4,5-P3 5'-phosphatase activity associated with Shc and Grb2. The insulin-regulated polyphosphoinositide 5'-phosphatase was not immunoreactive with antibody raised against the recently cloned SHIP 5'-phosphatase reported to associate with Shc and Grb2 in B lymphocytes. These data demonstrate that insulin causes formation of complexes containing a PI 3,4,5-P3 5'-phosphatase, and Shc or Grb2, or both, suggesting an important role of this enzyme in insulin signaling.
    Source

    J Biol Chem. 1996 Nov 22;271(47):29533-6.

    DOI
    10.1074/jbc.271.47.29533
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/42444
    PubMed ID
    8939879
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    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.271.47.29533
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