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J Biol Chem, Vol. 273, Issue 22, 13808-13818, May 29, 1998

Association of the Insulin Receptor with Phospholipase C- (PLC) in 3T3-L1 Adipocytes Suggests a Role for PLC in Metabolic Signaling by Insulin

From the UCSD/Whittier Diabetes Program, University of California San Diego, La Jolla, California 92093 and the Medical Research Service, Department of Veterans Affairs, Medical Center, San Diego, California 92161

Phospholipase C- (PLC) is the isozyme of PLC phosphorylated by multiple tyrosine kinases including epidermal growth factor, platelet-derived growth factor, nerve growth factor receptors, and nonreceptor tyrosine kinases. In this paper, we present evidence for the association of the insulin receptor (IR) with PLC. Precipitation of the IR with glutathione S-transferase fusion proteins derived from PLC and coimmunoprecipitation of the IR and PLC were observed in 3T3-L1 adipocytes. To determine the functional significance of the interaction of PLC and the IR, we used a specific inhibitor of PLC, U73122, or microinjection of SH2 domain glutathione S-transferase fusion proteins derived from PLC to block insulin-stimulated GLUT4 translocation. We demonstrate inhibition of 2-deoxyglucose uptake in isolated primary rat adipocytes and 3T3-L1 adipocytes pretreated with U73122. Antilipolytic effect of insulin in 3T3-L1 adipocytes is unaffected by U73122. U73122 selectively inhibits mitogen-activated protein kinase, leaving the Akt and p70 S6 kinase pathways unperturbed. We conclude that PLC is an active participant in metabolic and perhaps mitogenic signaling by the insulin receptor in 3T3-L1 adipocytes.

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