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J. Biol. Chem., Vol. 267, Issue 1, 31-34, 01, 1992
BR Conklin, O Chabre, YH Wong, AD Federman and HR Bourne
Gq mediates hormonal stimulation of phosphoinositide-specific phospholipase
C (PI-PLC). We mutated the alpha subunit of Gq (alpha q) to replace
arginine 183 with cysteine. Mutations that substitute cysteine for the
corresponding arginine residues of alpha s and alpha i2 constitutively
activate their respective effector pathways, creating the gsp and gip2
oncogenes. Transient expression of alpha q-R183C in COS-7 and HEK-293 cells
constitutively activates PI-PLC, but wild type (WT) alpha q does not. This
suggests that the mutated arginines in alpha s, alpha i2, and alpha q share
a common function in regulating the active state of these proteins and that
the alpha q gene may serve as a target for oncogenic mutations in human
tumors. In an attempt to develop an assay for receptor stimulation of
recombinant alpha q, we co- expressed receptors with alpha q-WT. We found
that the alpha 2- adrenoceptor stimulates PI-PLC activation in HEK-293
cells in a fashion that depends completely on co-expression of alpha q-WT.
These findings create an experimental model, similar to that provided for
alpha s by S49 cyc- cells, that should make it possible to analyze receptor
and effector coupling by mutant alpha q against a null background.
Recombinant Gq alpha. Mutational activation and coupling to receptors and phospholipase C
Department of Pharmacology, University of California, San Francisco 94143.
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I. Feoktistov, A. E. Goldstein, S. Ryzhov, D. Zeng, L. Belardinelli, T. Voyno-Yasenetskaya, and I. Biaggioni Differential Expression of Adenosine Receptors in Human Endothelial Cells: Role of A2B Receptors in Angiogenic Factor Regulation Circ. Res., March 22, 2002; 90(5): 531 - 538. [Abstract] [Full Text] [PDF]
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