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J Biol Chem, Vol. 273, Issue 15, 9234-9242, April 10, 1998
From the Second Department of Internal Medicine, Kobe University
School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650 and
§ Pharmacia Biotech,
Nishinakajima, Yodogawa-ku, Osaka, Japan
SHPS-1 is a receptor-like protein that undergoes
tyrosine phosphorylation and binds SHP-2, an SH2 domain-containing
protein tyrosine phosphatase, in response to insulin and other
mitogens. The overexpression of wild-type SHPS-1, but not of a mutant
SHPS-1 in which all four tyrosine residues in its cytoplasmic region were mutated to phenylalanine, markedly enhanced insulin-induced activation of mitogen-activated protein kinase in Chinese hamster ovary
cells that overexpress the human insulin receptor. Mutation of each
tyrosine residue individually revealed that the major sites of tyrosine
phosphorylation of SHPS-1 in response to insulin are
Tyr449 and Tyr473. In addition, mutation
of either Tyr449 or Tyr473 abolished the
insulin-induced tyrosine phosphorylation of SHPS-1 and its association
with SHP-2. Surface plasmon resonance analysis showed that glutathione
S-transferase fusion proteins containing the
NH2-terminal or COOH-terminal SH2 domains of SHP-2 bound
preferentially to phosphotyrosyl peptides corresponding to the
sequences surrounding Tyr449 or Tyr473,
respectively, of SHPS-1. Furthermore, phosphotyrosyl peptides containing Tyr449 or Tyr473 were effective
substrates for the phosphatase activity of recombinant SHP-2 in
vitro. Together, these results suggest that insulin may induce
phosphorylation of SHPS-1 at Tyr449 and Tyr473,
to which SHP-2 then binds through its NH2-terminal and
COOH-terminal SH2 domains, respectively. SHPS-1 may play a crucial role
both in the recruitment of SHP-2 from the cytosol to a site near the plasma membrane and in increasing its catalytic activity, thereby positively regulating the RAS-mitogen-activated protein kinase signaling cascade in response to insulin.
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