Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation

Goldschmidt-Clermont, P.J., Kim, J.W., Machesky, L.M. , Rhee, S.G. and Pollard, T.D. (1991) Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation. Science, 251(4998), pp. 1231-1233. (doi: 10.1126/science.1848725) (PMID:1848725)

Full text not currently available from Enlighten.


Epidermal growth factor and platelet-derived growth factor can stimulate the production of the second messenger inositol trisphosphate in responsive cells, but the biochemical pathway for these signaling events has been uncertain because the reactions have not been reconstituted with purified molecules in vitro. A reconstitution is described that requires not only the growth factor, its receptor with tyrosine kinase activity, and the soluble phospholipase C-gamma 1, but also the small soluble actin-binding protein profilin. Profilin binds to the substrate phosphatidylinositol 4,5-bisphosphate and inhibits its hydrolysis by unphosphorylated phospholipase C-gamma 1. Phosphorylation of phospholipase C-gamma 1 by the epidermal growth factor receptor tyrosine kinase overcomes the inhibitory effect of profilin and results in an effective activation of phospholipase C-gamma 1.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Machesky, Professor Laura
Authors: Goldschmidt-Clermont, P.J., Kim, J.W., Machesky, L.M., Rhee, S.G., and Pollard, T.D.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cancer Sciences
Journal Name:Science
Publisher:American Association for the Advancement of Science
ISSN (Online):1095-9203

University Staff: Request a correction | Enlighten Editors: Update this record