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J Biol Chem, Vol. 273, Issue 47, 31186-31190, November 20, 1998
-gated Potassium Channels
From the Department of Molecular Pharmacology and Biological
Chemistry, Northwestern University Medical
School, Chicago, Illinois 60611
Here we report novel effects of regulators of G
protein signaling (RGS) on G protein-regulated ion channels. RGS3 and
RGS4 induced a substantial increase in currents through the
G
-regulated inwardly rectifying K+ channels,
IK(ACh), in the absence of receptor activation.
Concomitantly, the amount of current that could be activated by agonist
was reduced. Pretreatment with pertussis toxin or a muscarinic receptor
antagonist abolished agonist-induced currents but did not modify RGS
effects. Cotransfection of cells with a G-binding protein
significantly reduced the RGS4-induced basal
IK(ACh) currents. The RGS proteins also
modified the properties of another G effector, the N-type Ca2+ channels. These observations strongly suggest that RGS
proteins increase the availability of G in addition to their
previously described GTPase-activating function.
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