A new tyrosine-phosphorylated 97-kDa adaptor protein mediates interleukin-2-induced association of SHP-2 with p85-phosphatidylinositol 3-kinase in human T lymphocytes.

The Journal of Biological Chemistry
F GesbertJ H Bertoglio

Abstract

Interleukin (IL)-2 is a major cytokine that controls differentiation and proliferation of T lymphocytes. In this report we characterize an as yet unidentified 97-kDa protein that is a major tyrosine kinase substrate in IL-2-stimulated cells. pp97 was found to associate with the p85.p110 phosphatidylinositol 3-kinase complex, the Src homology 2 (SH2) domain-containing tyrosine phosphatase SHP-2, and the adaptor molecules CrkL and Grb2. We demonstrate that these interactions are directly mediated through the SH2 domains of CrkL, p85, and SHP-2 and through the SH3 domains of Grb2. pp97 was found to mediate the IL-2-induced interaction between p85 and both a phosphorylated and a non-phosphorylated form of SHP-2. In this study we show that pp97 behaves as a docking protein and associates with at least CrkL, p85, and SHP-2 in the same multimolecular complex. We thus characterized pp97 as a new tyrosine kinase substrate in human T lymphocytes which might play a central role in the regulation of several pathways activated by IL-2.

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Citations

May 25, 2010·The Journal of Biological Chemistry·Pavel Montes de OcaFranck Gesbert
Sep 13, 2000·Molecular and Cellular Biology·H GuB G Neel
Dec 1, 2000·Biochemical and Biophysical Research Communications·A OdaK Ikebuchi
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Jul 16, 2010·Current Opinion in Organ Transplantation·Antoine DurrbachBernard Charpentier
Jul 13, 2004·Biochimica Et Biophysica Acta·Alan K Howe
Apr 12, 2002·FEBS Letters·Yan Liu, Larry R Rohrschneider
Aug 27, 2005·The Journal of Biological Chemistry·Qing DengJoseph T Barbieri
Apr 24, 1999·FEBS Letters·M Delespine-CarmagnatJ Bertoglio
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Nov 12, 2019·Frontiers in Immunology·Charlène NiogretGreta Guarda
Jun 15, 2000·Experimental Cell Research·C SunshineK L Kirk

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