%0 Journal Article %1 Lohse2007b %A Lohse, M. J. %A Hoffmann, C. %A Nikolaev, V. O. %A Vilardaga, J. P. %A Bunemann, M. %D 2007 %J Adv Protein Chem %K *Signal Animals Cell Energy Fluorescence G-Protein-Coupled/*chemistry/*metabolism GTP-Binding Heterotrimeric Humans Kinetics Proteins/chemistry/metabolism Resonance Survival Transduction Transfer/*methods Receptor %P 167-88 %T Kinetic analysis of G protein-coupled receptor signaling using fluorescence resonance energy transfer in living cells %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17854658 %V 74 %X We describe and review methods for the kinetic analysis of G protein-coupled receptor (GPCR) activation and signaling that are based on optical methods. In particular, we describe the use of fluorescence resonance energy transfer (FRET) as a means of analyzing conformational changes within a single protein (for example a receptor) or between subunits of a protein complex (such as a G protein heterotrimer) and finally between distinct proteins (such as a receptor and a G protein). These methods allow the analysis of signaling kinetics in intact cells with proteins that retain their essential functional properties. They have produced a number of unexpected results: fast receptor activation kinetics in the millisecond range, similarly fast kinetics for receptor-G protein interactions, but much slower activation kinetics for G protein activation.

@article{Lohse2007b, abstract = {We describe and review methods for the kinetic analysis of G protein-coupled receptor (GPCR) activation and signaling that are based on optical methods. In particular, we describe the use of fluorescence resonance energy transfer (FRET) as a means of analyzing conformational changes within a single protein (for example a receptor) or between subunits of a protein complex (such as a G protein heterotrimer) and finally between distinct proteins (such as a receptor and a G protein). These methods allow the analysis of signaling kinetics in intact cells with proteins that retain their essential functional properties. They have produced a number of unexpected results: fast receptor activation kinetics in the millisecond range, similarly fast kinetics for receptor-G protein interactions, but much slower activation kinetics for G protein activation.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Lohse, M. J. and Hoffmann, C. and Nikolaev, V. O. and Vilardaga, J. P. and Bunemann, M.}, biburl = {https://www.bibsonomy.org/bibtex/22a2695dd59400daa891326e21ca2f3ff/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {812969b89347cf79a29101b5fccc50c8}, intrahash = {2a2695dd59400daa891326e21ca2f3ff}, issn = {0065-3233 (Print) 0065-3233 (Linking)}, journal = {Adv Protein Chem}, keywords = {*Signal Animals Cell Energy Fluorescence G-Protein-Coupled/*chemistry/*metabolism GTP-Binding Heterotrimeric Humans Kinetics Proteins/chemistry/metabolism Resonance Survival Transduction Transfer/*methods Receptor}, note = {Lohse, Martin J Hoffmann, Carsten Nikolaev, Viacheslav O Vilardaga, Jean-Pierre Bunemann, Moritz Research Support, Non-U.S. Gov't Review United States Advances in protein chemistry Adv Protein Chem. 2007;74:167-88.}, pages = {167-88}, shorttitle = {Kinetic analysis of G protein-coupled receptor signaling using fluorescence resonance energy transfer in living cells}, timestamp = {2010-12-14T18:20:06.000+0100}, title = {Kinetic analysis of G protein-coupled receptor signaling using fluorescence resonance energy transfer in living cells}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17854658}, volume = 74, year = 2007 }