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J Biol Chem, Vol. 275, Issue 6, 4283-4289, February 11, 2000
From the Dorrance H. Hamilton Research Laboratories, Division of
Endocrinology, Diabetes and Metabolic Diseases, Department of Medicine,
Jefferson Medical College of Thomas Jefferson University,
Philadelphia, Pennsylvania 19107
Regulation of the steady-state tyrosine
phosphorylation of the insulin receptor and its postreceptor substrates
are essential determinants of insulin signal transduction. However,
little is known regarding the molecular interactions that influence the balance of these processes, especially the phosphorylation state of
postinsulin receptor substrates, such as insulin receptor substrate-1 (IRS-1). The specific activity of four candidate protein-tyrosine phosphatases (protein-tyrosine phosphatase 1B (PTP1B), SH2
domain-containing PTPase-2 (SHP-2), leukocyte common antigen-related
(LAR), and leukocyte antigen-related phosphatase) (LRP) toward IRS-1
dephosphorylation was studied using recombinant proteins in
vitro. PTP1B exhibited the highest specific activity (percentage
dephosphorylated per µg per min), and the enzyme activities varied
over a range of 5.5 × 103. When evaluated as a ratio
of activity versus IRS-1 to that versus p-nitrophenyl phosphate, PTP1B remained significantly more
active by 3.1-293-fold, respectively. Overlay blots with recombinant Src homology 2 domains of IRS-1 adaptor proteins showed that the loss
of IRS-1 binding of Crk, GRB2, SHP-2, and the p85 subunit of
phosphatidylinositol 3'-kinase paralleled the rate of overall IRS-1
dephosphorylation. Further studies revealed that the adaptor protein
GRB2 strongly promoted the formation of a stable protein complex
between tyrosine-phosphorylated IRS-1 and catalytically inactive PTP1B,
increasing their co-immunoprecipitation from an equimolar solution by
13.5 ± 3.3-fold (n = 7; p < 0.01). Inclusion of GRB2 in a reaction mixture of IRS-1 and active
PTP1B also increased the overall rate of IRS-1 tyrosine
dephosphorylation by 2.7-3.9-fold (p < 0.01). These
results provide new insight into novel molecular interactions involving
PTP1B and GRB2 that may influence the steady-state capacity of IRS-1 to
function as a phosphotyrosine scaffold and possibly affect the balance
of postreceptor insulin signaling.
Tyrosine Dephosphorylation and Deactivation of Insulin Receptor
Substrate-1 by Protein-tyrosine Phosphatase 1B
POSSIBLE FACILITATION BY THE FORMATION OF A TERNARY COMPLEX WITH
THE GRB2 ADAPTOR PROTEIN*
,
*
This work was supported by National Institutes of Health
Grant R01-DK43396 (to B. J. G.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom all correspondence should be addressed: Division of
Endocrinology, Diabetes and Metabolic Diseases, Jefferson Medical College, Room 349 Alumni Hall, 1020 Locust St., Philadelphia, PA 19107. Tel.: 215-503-1272; Fax: 215-923-7932; E-mail:
Barry.Goldstein@mail.tju.edu.
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