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Mol. Cell. Biol., 12 1996, 6887-6899, Vol 16, No. 12
Y Fujioka, T Matozaki, T Noguchi, A Iwamatsu, T Yamao, N Takahashi, M Tsuda, T Takada and M Kasuga
Protein tyrosine phosphatases (PTPases), such as SHP-1 and SHP-2, that
contain Src homology 2 (SH2) domains play important roles in growth factor
and cytokine signal transduction pathways. A protein of approximately 115
to 120 kDa that interacts with SHP-1 and SHP-2 was purified from
v-src-transformed rat fibroblasts (SR-3Y1 cells), and the corresponding
cDNA was cloned. The predicted amino acid sequence of the encoded protein,
termed SHPS-1 (SHP substrate 1), suggests that it is a glycosylated
receptor-like protein with three immunoglobulin-like domains in its
extracellular region and four YXX(L/V/I) motifs, potential tyrosine
phosphorylation and SH2-domain binding sites, in its cytoplasmic region.
Various mitogens, including serum, insulin, and lysophosphatidic acid, or
cell adhesion induced tyrosine phosphorylation of SHPS-1 and its subsequent
association with SHP-2 in cultured cells. Thus, SHPS-1 may be a direct
substrate for both tyrosine kinases, such as the insulin receptor kinase or
Src, and a specific docking protein for SH2-domain-containing PTPases. In
addition, we suggest that SHPS-1 may be a potential substrate for SHP-2 and
may function in both growth factor- and cell adhesion-induced cell
signaling.
Copyright © 1996, American Society for Microbiology
A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain- containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion
Second Department of Internal Medicine, Kobe University School of Medicine, Chuo-ku, Japan.
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