Rhodopsin self-associates in asolectin liposomes

Steven E. Mansoor, Krzysztof Palczewski, David Farrens

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

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 A 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.

Original languageEnglish (US)
Pages (from-to)3060-3065
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume103
Issue number9
DOIs
StatePublished - Feb 28 2006

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Rhodopsin
Liposomes
Energy Transfer
Luminescence
Transducin
Membranes
asolectin
GTP-Binding Proteins

Keywords

  • FRET
  • G protein-coupled receptor
  • GPCR dimer
  • Luminescence resonance energy transfer
  • Signal transduction

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Rhodopsin self-associates in asolectin liposomes. / Mansoor, Steven E.; Palczewski, Krzysztof; Farrens, David.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, No. 9, 28.02.2006, p. 3060-3065.

Research output: Contribution to journalArticle

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