Rhodopsin Self-Associates in Asolectin Liposomes

We show that the photoreceptor rhodopsin (Rh) can exist in the membrane as a dimer or multimer using luminescence resonance energy transfer and FRET methods. Our approach looked for interactions between Rh molecules reconstituted into asolectin liposomes. The low receptor density used in the measure...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 103; no. 9; pp. 3060 - 3065
Main Authors Mansoor, Steven E., Palczewski, Krzysztof, Farrens, David L.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 28.02.2006
National Acad Sciences
Subjects
Biochemistry
Biological Sciences
Biology
Cells
Density
Dimers
Efficiency metrics
Energy transfer
Fluorescence
Fluorescence Resonance Energy Transfer
Genes, Reporter - genetics
Light
Lipids
Liposomes
Liposomes - chemistry
Membranes
Molecules
Phosphatidylcholines
Phospholipids
Protein Binding
Proteins
Receptors
Rhodopsin - chemistry
Rhodopsin - genetics
Rhodopsin - metabolism
Rhodopsin - ultrastructure
Signal transduction
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Summary:We show that the photoreceptor rhodopsin (Rh) can exist in the membrane as a dimer or multimer using luminescence resonance energy transfer and FRET methods. Our approach looked for interactions between Rh molecules reconstituted into asolectin liposomes. The low receptor density used in the measurements ensured minimal receptor crowding and artifactual association. The fluorescently labeled Rh molecules were fully functional, as measured by their ability to activate the G protein transducin. The luminescence resonance energy transfer measurements revealed a distance of 47-50 Å between Rh molecules. The measured efficiency of FRET between receptors was close to the theoretical maximum possible, indicating nearly quantitative Rh-Rh association. Together, these results provide compelling evidence that Rh spontaneously self-associates in membranes.
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Author contributions: S.E.M. and D.L.F. designed research; S.E.M. performed research; S.E.M. and D.L.F. analyzed data; and S.E.M., K.P., and D.L.F. wrote the paper.
Communicated by H. Gobind Khorana, Massachusetts Institute of Technology, Cambridge, MA, December 20, 2005
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0511010103