M.I. Wahl, S. Nishibe, P.-G. Suh, S.G. Rhee, G. Carpenter, "Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium," PNAS, 86, 1568-72, March 1989.
Matthew I. Wahl (Vanderbilt University School of Medicine, Nashville, Tenn.): "While an earlier paper from our group (Science, 241:968-70, 1988) provided preliminary evidence, this paper demonstrated directly that a particular phospholipase C (PLC) isozyme, PLC-ç1 (PLC-II), is phosphorylated on tyrosine residues in epidermal growth factor (EGF)-treated cells. PLC-ç1 was the first regulatory enzyme capable of generating important `second messenger' molecules to be identified as a substrate for a tyrosine kinase. Almost all previous studies suggested that hormone-stimulated increases in cellular phospholipase C activity occurred indirectly, mediated by an unidentified guanine nucleotide binding protein (GTP) or proteins. Work by several groups has demonstrated direct, selective PLC-ç1 tyrosine phosphorylation by the epidermal growth factor and platelet-derived growth factor receptors, suggesting the ...
