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First published online June 20, 2006
doi: 10.1242/10.1242/jcs.03021

Journal of Cell Science 119, 2807-2818 (2006)
Published by The Company of Biologists 2006
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Research Article

Heterotrimeric G proteins form stable complexes with adenylyl cyclase and Kir3.1 channels in living cells

R. Victor Rebois1,*,1,{ddagger}, Mélanie Robitaille2,3,*, Céline Galés2,*, Denis J. Dupré3, Alessandra Baragli3, Phan Trieu3, Nathalie Ethier3, Michel Bouvier2 and Terence E. Hébert2,3,{ddagger}

1 Laboratory of Cellular Biology, 5 Research Court, National Institute of Deafness and Communicative Disorders, National Institutes of Health, Rockville, MD 20850, USA
2 Département de Biochimie, Université de Montréal, Montréal, Québec, H3C 3J7 Canada
3 Department of Pharmacology and Therapeutics, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montréal, Québec, H3G 1Y6, Canada

{ddagger} Authors for correspondence (e-mail: reboisv{at}nidcd.nih.gov; terence.hebert{at}mcgill.ca)

Accepted 19 April 2006

Bioluminescence resonance energy transfer (BRET) and co-immunoprecipitation experiments revealed that heterotrimeric G proteins and their effectors were found in stable complexes that persisted during signal transduction. Adenylyl cyclase, Kir3.1 channel subunits and several G-protein subunits (G{alpha}s, G{alpha}i, Gß1 and G{gamma}2) were tagged with luciferase (RLuc) or GFP, or the complementary fragments of YFP (specifically Gß1-YFP1-158 and G{gamma}2-YFP159-238, which heterodimerize to produce fluorescent YFP-Gß1{gamma}2). BRET was observed between adenylyl-cyclase-RLuc or Kir3.1-RLuc and GFP-G{gamma}2, GFP-Gß1 or YFP-Gß1{gamma}2. G{alpha} subunits were also stably associated with both effectors regardless of whether or not signal transduction was initiated by a receptor agonist. Although BRET between effectors and Gß{gamma} was increased by receptor stimulation, our data indicate that these changes are likely to be conformational in nature. Furthermore, receptor-sensitive G-protein-effector complexes could be detected before being transported to the plasma membrane, providing the first direct evidence for an intracellular site of assembly.

Key words: Adenylyl cyclase, ß2-adrenergic receptor, BiFC, BRET, G-protein-coupled inwardly rectifying K+ channels, Heterotrimeric G proteins


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