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(Received for publication, March 27, 1996, and in revised form, July 8, 1996)
From the Second Department of Internal Medicine, Kobe University
School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650, Japan
SH-PTP2, a non-transmembrane-type
protein-tyrosine phosphatase with two Src homology 2 domains, was
previously shown to play a positive signaling role in the
insulin-induced activation of Ras and mitogen-activated protein kinase.
SH-PTP2 was shown to associate with a 115-kDa tyrosine-phosphorylated
protein (pp115), as well as with insulin receptor substrate 1, in
insulin-stimulated Chinese hamster ovary cells that overexpress human
insulin receptors (CHO-IR cells). In vivo and in
vitro binding experiments revealed that SH-PTP2 bound to pp115
through one or both of its SH2 domains. The pp115 protein was partially
purified from insulin-stimulated CHO-IR cells that overexpress a
catalytically inactive SH-PTP2 by a combination of immunoaffinity and
lectin-affinity chromatography. A monoclonal antibody to pp115 was then
generated by injecting the partially purified protein into mice.
Experiments with this monoclonal antibody revealed that pp115 is a
transmembrane protein with a domain exposed on the cell surface and
that it binds to SH-PTP2 in response to insulin. The insulin receptor
kinase appeared to phosphorylate pp115 on tyrosine residues both
in vivo and in vitro. The extent of tyrosine
phosphorylation of pp115 associated with SH-PTP2 was greatly increased
in CHO-IR cells that overexpress catalytically inactive SH-PTP2
compared with that observed in CHO-IR cells overexpressing wild-type
SH-PTP2. Furthermore, recombinant SH-PTP2 preferentially
dephosphorylated pp115 in vitro, indicating that SH-PTP2
may catalyze the dephosphorylation of phosphotyrosine residues in pp115
after it binds to this protein. These results suggest that pp115 may
act as a transmembrane anchor to which SH-PTP2 binds in response to
insulin. Furthermore, pp115 may be a physiological substrate for both
the insulin receptor kinase and SH-PTP2.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27652-27658
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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