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Originally published In Press as doi:10.1074/jbc.M108927200 on November 1, 2001

J. Biol. Chem., Vol. 277, Issue 1, 338-344, January 4, 2002
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Muscarinic Receptors Mediate Phospholipase C-dependent Activation of Protein Kinase B via Ca2+, ErbB3, and Phosphoinositide 3-Kinase in 1321N1 Astrocytoma Cells*

Xiuwen TangDagger §, Ian H. BattyDagger , and C. Peter Downes

From the Division of Cell Signalling, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland

In 1321N1 astrocytoma cells, heterotrimeric G-protein-coupled receptors that activate phosphoinositide-specific phospholipase Cbeta (PLCbeta ) isoforms via Gq, induced a prolonged activation of protein kinase B (PKB) after a short delay. For example, the effect of carbachol acting on M3 muscarinic receptors is blocked by wortmannin, suggesting it is mediated via a phosphoinositide 3-kinase (PI 3-kinase). In support of this, carbachol increased PI 3-kinase activity in PI 3-kinase (p85) immunoprecipitates. The pathway linking PLC-coupled receptors to PI 3-kinase was deduced to involve phosphoinositide hydrolysis and Ca2+-dependent ErbB3 transactivation but not protein kinase C on the basis of the following evidence: (i) inhibition of carbachol stimulated PLC by pretreatment with the phorbol ester phorbol 12-myristate 13-acetate concomitantly reduced PKB activity, whereas stimulation of other PLC-coupled receptors also activated PKB; (ii) Ca2+ ionophores and thapsigargin stimulated PKB activity in a wortmannin-sensitive manner, whereas bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid blocked carbachol-stimulated PKB activity; (iii) phorbol 12-myristate 13-acetate alone did not activate PKB, whereas a protein kinase C inhibitor did not prevent the activation of PKB by carbachol; and (iv) carbachol stimulated ErbB3-tyrosine phosphorylation and association with p85, and both these and PKB activity were blocked by tyrphostin AG1478, an epidermal growth factor receptor-tyrosine kinase inhibitor. These experiments define a novel pathway linking Gq-coupled G-protein-coupled receptors to the activation of PI 3-kinase and PKB.

* This work was supported by the Medical Research Council (United Kingdom).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger These authors contributed equally to this work.

§ To whom correspondence should be addressed. Tel.: 44-1382-344729; Fax: 44-1382-348210; E-mail: x.tang@dundee.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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