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J Biol Chem, Vol. 274, Issue 6, 3549-3556, February 5, 1999
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From the Departments of Regulators of G protein signaling (RGS) proteins
accelerate GTP hydrolysis by G Physiology and
¶ Pharmacology, University of Texas Southwestern Medical
Center, Dallas, Texas 75235, Millenium Pharmaceuticals,
Inc., Cambridge, Massachusetts 02139, and the ** Institute for
Pharmacology, Klinikum Benjamin Franklin, Freie Universität
Berlin, 14159 Berlin, Germany
subunits, thereby attenuating
signaling. RGS4 is a GTPase-activating protein for Gi
and Gq class subunits. In the present study, we used
knockouts of Gq class genes in mice to evaluate the potency
and selectivity of RGS4 in modulating Ca2+ signaling
transduced by different Gq-coupled receptors. RGS4 inhibited phospholipase C activity and Ca2+ signaling in a
receptor-selective manner in both permeabilized cells and cells
dialyzed with RGS4 through a patch pipette.
Receptor-dependent inhibition of Ca2+ signaling
by RGS4 was observed in acini prepared from the rat and mouse pancreas.
The response of mouse pancreatic acini to carbachol was about 4- and
33-fold more sensitive to RGS4 than that of bombesin and
cholecystokinin (CCK), respectively. RGS1 and RGS16 were also potent
inhibitors of Gq-dependent Ca2+
signaling and acted in a receptor-selective manner. RGS1 showed approximately 1000-fold higher potency in inhibiting carbachol than
CCK-dependent signaling. RGS16 was as effective as RGS1 in inhibiting carbachol-dependent signaling but only partially
inhibited the response to CCK. By contrast, RGS2 inhibited the response to carbachol and CCK with equal potency. The same pattern of
receptor-selective inhibition by RGS4 was observed in acinar cells from
wild type and several single and double Gq class knockout
mice. Thus, these receptors appear to couple Gq class subunit isotypes equally. Difference in receptor selectivity of RGS
proteins action indicates that regulatory specificity is conferred by
interaction of RGS proteins with receptor complexes.
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K. M. Druey, O. Ugur, J. M. Caron, C.-K. Chen, P. S. Backlund, and T. L. Z. Jones Amino-terminal Cysteine Residues of RGS16 Are Required for Palmitoylation and Modulation of Gi- and Gq-mediated Signaling J. Biol. Chem., June 25, 1999; 274(26): 18836 - 18842. [Abstract] [Full Text] [PDF]
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