NDLI: Gi protein activation in intact cells involves subunit rearrangement rather than dissociation.

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Gi protein activation in intact cells involves subunit rearrangement rather than dissociation.

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Gi protein activation in intact cells involves subunit rearrangement rather than dissociation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bünemann, Moritz Frank, Monika Lohse, Martin J.
Description	Author Affiliation: Bünemann M ( Department of Pharmacology and Toxicology, University of Würzburg, Versbacherstrasse 9, 97078 Würzburg, Germany. m-buenemann@toxi.uni-wuerzburg.de);
Abstract	G protein-coupled receptors transduce diverse extracellular signals, such as neurotransmitters, hormones, chemokines, and sensory stimuli, into intracellular responses through activation of heterotrimeric G proteins. G proteins play critical roles in determining specificity and kinetics of subsequent biological responses by modulation of effector proteins. We have developed a fluorescence resonance energy transfer (FRET)-based assay to directly measure mammalian G protein activation in intact cells and found that Gi proteins activate within 1-2 s, which is considerably slower than activation kinetics of the receptors themselves. More importantly, FRET measurements demonstrated that Galphai- and Gbetagamma-subunits do not dissociate during activation, as has been previously postulated. Based on FRET measurements between Galphai-yellow fluorescent protein and Gbetagamma-subunits that were fused to cyan fluorescent protein at various positions, we conclude that, instead, G protein subunits undergo a molecular rearrangement during activation. The detection of a persistent heterotrimeric composition during G protein activation will impact the understanding of how G proteins achieve subtype-selective coupling to effectors. This finding will be of particular interest for unraveling Gbetagamma-induced signaling pathways.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	GTP-Binding Protein Alpha Subunits, Gi-Go Metabolism Potassium Channels, Inwardly Rectifying Animals Fluorescence Resonance Energy Transfer G Protein-Coupled Inwardly-Rectifying Potassium Channels Genetics Genes, Reporter Green Fluorescent Proteins Luminescent Proteins Mutagenesis, Site-Directed Potassium Channels Physiology Protein Subunits Chemistry Recombinant Proteins Transfection Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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