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Vol. 273, Issue 2, 729-735, January 9, 1998
From the Joslin Diabetes Center and Department of Medicine, Harvard
Medical School, Boston, Massachusetts 02215 and § ARIAD
Pharmaceuticals, Inc., Cambridge, Massachusetts 02139
SH2 domain proteins transmit intracellular
signals initiated by activated tyrosine kinase-linked receptors. Recent
three-dimensional structures suggest mechanisms by which tandem SH2
domains might confer higher specificity than individual SH2 domains. To
test this, binding studies were conducted with tandem domains from the
five signaling enzymes: phosphatidylinositol 3-kinase p85, ZAP-70, Syk,
SHP-2, and phospholipase C-
1. Bisphosphorylated TAMs (tyrosine-based
activation motifs) were derived from biologically relevant sites in
platelet-derived growth factor, T cell, B cell, and high affinity IgE
receptors and the receptor substrates IRS-1 (insulin receptor
substrate-1) and SHPS-1/SIRP. Each tandem SH2 domain binds a distinct
TAM corresponding to its appropriate biological partner with highest
affinity (0.5-3.0 nM). Alternative TAMs bind the
tandem SH2 domains with 1,000- to >10,000-fold lower affinity than
biologically relevant TAMs. This level of specificity is significantly
greater than the ~20-50-fold typically seen for individual SH2
domains. We conclude that high biological specificity is conferred by
the simultaneous interaction of two SH2 domains in a signaling enzyme
with bisphosphorylated TAMs in activated receptors and substrates.
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J. M. Cunnick, L. Mei, C. A. Doupnik, and J. Wu Phosphotyrosines 627 and 659 of Gab1 Constitute a Bisphosphoryl Tyrosine-based Activation Motif (BTAM) Conferring Binding and Activation of SHP2 J. Biol. Chem., June 22, 2001; 276(26): 24380 - 24387. [Abstract] [Full Text] [PDF]
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