NDLI: Phospholipase C-gamma 1 binding to intracellular receptors for activated protein kinase C.

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Phospholipase C-gamma 1 binding to intracellular receptors for activated protein kinase C.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Disatnik, M. H. Jones, G. Hernandez-sotomayor, S. M. Carpenter, G. Mochly-rosen, D.
Description	Author Affiliation: Disatnik MH ( Department of Molecular Pharmacology, School of Medicine, Stanford University, CA 94305-5332.);
Abstract	Phospholipase C-gamma 1 (PLC-gamma 1; EC 3.1.4.11) hydrolyzes phosphatidylinositol 4,5-bisphosphate to generate diacylglycerol and inositol 1,4,5-trisphosphate and is activated in response to growth factor stimulation and tyrosine phosphorylation. Concomitantly, the enzyme translocates from the cytosol to the particulate cell fraction. A similar process of activation-induced translocation from the cytosol to the cell particulate fraction has also been described for protein kinase C (PKC). We have previously shown that activated PKC binds to specific receptor proteins, receptors for activated C kinase, or RACKs, of approximately 30 kDa. Here, we show that PLC-gamma 1 bound to these RACKs and inhibited subsequent PKC binding to RACKs. However, unlike PKC, the binding of PLC-gamma 1 to RACKs did not require phospholipids and calcium. After epidermal growth factor treatment of intact A-431 cells, the binding of PLC-gamma 1 to RACKs increased as compared with PLC-gamma 1 from control cells. This increase in PLC-gamma 1 binding to RACKs was due to the phosphorylation of PLC-gamma 1. Additional data indicated that PLC-gamma 1 binds to RACKs in solution; epidermal growth factor receptor-dependent PLC-gamma 1 phosphorylation and activation decreased in the presence of RACKs. It is possible that, in vivo, PLC-gamma 1 associates with RACKs or with other PLC-gamma 1-specific anchoring proteins in the particulate cell fraction. Since a PKC C2 homologous region is present in PLC-gamma 1, the C2 region may mediate the activation-induced translocation of the enzyme to the cell particulate fraction and the anchoring protein-PLC-gamma 1 complex may be the active translocated form of PLC-gamma 1.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Isoenzymes Metabolism Protein Kinase C Receptors, Cell Surface Type C Phospholipases Amino Acid Sequence Binding Sites Binding, Competitive Cell Line Enzyme Activation Epidermal Growth Factor Pharmacology In Vitro Techniques Genetics Immunology Molecular Sequence Data Phospholipase C Gamma Phosphorylation Subcellular Fractions Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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