A. Kashishian, A. Kazlauskas, J.A. Cooper, "Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo," The EMBO Journal, 11[4]:1373-82, 1992.

Adam Kashishian (Fred Hutchinson Cancer Research Center, Seattle): "The question of the specificity of Src homology 2 (SH2) domain/phosphotyrosine interactions has been an important one since the ability of the SH2 domains to bind phosphotyrosine- containing peptides was first shown. Different growth factor receptors were known to bind different constellations of SH2 domain-containing proteins. Was this a function of differences in receptor primary sequence, their locations in the cell, or, possibly, the specificity of the protein kinase domain of the receptor? As we mapped and mutated phosphorylation sites in the platelet-derived growth factor (PDGF) receptor, we found a dramatic difference in interactions of three tyrosines in the `kinase-insert' region. Mutation of either Tyr740 or 751 strongly reduced binding of an SH2 protein...

Interested in reading more?

Become a Member of

Receive full access to digital editions of The Scientist, as well as TS Digest, feature stories, more than 35 years of archives, and much more!
Already a member?