D. Anderson, C.A. Koch, L. Grey, C. Ellis, et al., "Binding of SH2 domains of phospholipase Cg1, GAP, and Src to activated growth factor receptors," Science, 250:979-82, 1990.
Tony Pawson (Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto): "Many of the hormones that control cell growth, differentiation, and metabolism in the adult, and development in the embryo, bind to the extracellular region of receptors that span the plasma membrane. These receptors contain a cytoplasmic protein kinase catalytic domain that phosphorylates tyrosine residues. The first thing a stimulated receptor does is to extensively phosphorylate its own tyrosine residues.
"Normally, these receptor tyrosine kinases are active only when they are engaged by the appropriate growth factor. However, structural alterations, resulting from cancer-causing mutations in the relevant genes, can render these receptors active even in the absence of any growth factor. Such aberrantly active receptors can trigger unrestricted, cancerous cell growth.
"This much ...
