%0 Journal Article %1 Bunemann1998 %A Bunemann, M. %A Hosey, M. M. %D 1998 %J J Biol Chem %K *GTPase-Activating *Potassium *RGS Antagonists/pharmacology Bordetella/pharmacology Calcium Channels Channels, Channels/agonists/genetics/*metabolism Channels/metabolism Conductivity Electric Factors, G GTP-Binding Inwardly Inwardly-Rectifying Muscarinic Pertussis Potassium Protein-Coupled Proteins Proteins/metabolism Recombinant Rectifying Signal Toxin Transduction Virulence %N 47 %P 31186-90 %T Regulators of G protein signaling (RGS) proteins constitutively activate Gbeta gamma-gated potassium channels %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9813023 %V 273 %X 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 Gbeta gamma-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 Gbetagamma-binding protein significantly reduced the RGS4-induced basal IK(ACh) currents. The RGS proteins also modified the properties of another Gbeta gamma effector, the N-type Ca2+ channels. These observations strongly suggest that RGS proteins increase the availability of Gbeta gamma in addition to their previously described GTPase-activating function.

@article{Bunemann1998, abstract = {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 Gbeta gamma-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 Gbetagamma-binding protein significantly reduced the RGS4-induced basal IK(ACh) currents. The RGS proteins also modified the properties of another Gbeta gamma effector, the N-type Ca2+ channels. These observations strongly suggest that RGS proteins increase the availability of Gbeta gamma in addition to their previously described GTPase-activating function.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Bunemann, M. and Hosey, M. M.}, biburl = {https://www.bibsonomy.org/bibtex/288876a074e3cd5b3d07e652f7e4a780e/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {f6ef844725a2a5f560f1bb25df079ace}, intrahash = {88876a074e3cd5b3d07e652f7e4a780e}, issn = {0021-9258 (Print) 0021-9258 (Linking)}, journal = {J Biol Chem}, keywords = {*GTPase-Activating *Potassium *RGS Antagonists/pharmacology Bordetella/pharmacology Calcium Channels Channels, Channels/agonists/genetics/*metabolism Channels/metabolism Conductivity Electric Factors, G GTP-Binding Inwardly Inwardly-Rectifying Muscarinic Pertussis Potassium Protein-Coupled Proteins Proteins/metabolism Recombinant Rectifying Signal Toxin Transduction Virulence}, month = {Nov 20}, note = {Bunemann, M Hosey, M M HL50121/HL/NHLBI NIH HHS/United States Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. United states The Journal of biological chemistry J Biol Chem. 1998 Nov 20;273(47):31186-90.}, number = 47, pages = {31186-90}, shorttitle = {Regulators of G protein signaling (RGS) proteins constitutively activate Gbeta gamma-gated potassium channels}, timestamp = {2010-12-14T18:21:42.000+0100}, title = {Regulators of G protein signaling (RGS) proteins constitutively activate Gbeta gamma-gated potassium channels}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9813023}, volume = 273, year = 1998 }