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J Biol Chem, Vol. 273, Issue 29, 18273-18281, July 17, 1998
From INSERM Unit 461, Faculté de Pharmacie Paris-XI,
92296 Châtenay-Malabry, France
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.
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
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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