Phospholipase C-gamma1: regulation of enzyme function and role in growth factor-dependent signal transduction.
Phospholipase C(gamma)1 (PLC-gamma1), a tyrosine kinase substrate, is a multi-domain molecule that modulates the intracellular levels of the second messenger molecules: Ca2+ and diacylglycerol. Although a wide variety of growth factor receptor tyrosine kinases phosphorylate and activate PLC-gamma1, the biological role and necessity of this signal transduction element in mitogenesis has remained unclear. Recent results, however, point to a more essential role than was suggested by initial studies. Also, biochemical studies have indicated a putative means for the intramolecular repression of PLC-gamma1 activity and provide a means for interpreting activation signals through a derepression mechanism.
Kamat
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Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Carpenter
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G
D000818:Animals; D004789:Enzyme Activation; D006133:Growth Substances / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000502:physiology*; D008322:Mammals; D051379:Mice; D051966:Phospholipase C gamma; D015398:Signal Transduction; D010738:Type C Phospholipases / Q000737:chemistry* / Q000502:physiology*
D006133:Growth Substances; D007527:Isoenzymes; D010738:Type C Phospholipases; D051966:Phospholipase C gamma