Growth factor signaling pathways: phosphoinositide metabolism and phosphorylation of phospholipase C.
Recent demonstrations of growth factor-stimulated increases in cellular phosphoinositide metabolism suggest that regulatory enzymes of this important signaling pathway may be substrates for growth factor receptor tyrosine kinases. Studies employing phosphotyrosine antibodies, specific phospholipase C antibodies, and purified phospholipase C proteins support the conclusion that the 145-kD phospholipase C-gamma 1 isoenzyme is rapidly and selectively phosphorylated by the activated epidermal growth factor and platelet-derived growth factor receptors. The selective interaction of these receptors with phospholipase C-gamma 1 suggests a novel, direct mechanism for agonist stimulation of phosphoinositide metabolism.
Wahl
M I
MI
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
Nishibe
S
S
Carpenter
G
G
D006133:Growth Substances / Q000378:metabolism*; D006801:Humans; D010716:Phosphatidylinositols / Q000378:metabolism*; D010766:Phosphorylation; D015398:Signal Transduction / Q000502:physiology*; D010738:Type C Phospholipases / Q000378:metabolism*
D006133:Growth Substances; D010716:Phosphatidylinositols; D010738:Type C Phospholipases