Monomeric rhodopsin is the minimal functional unit required for arrestin binding

Hisao Tsukamoto, Abhinav Sinha, Mark DeWitt, David Farrens

Research output: Contribution to journalArticle

70 Citations (Scopus)

Abstract

We have tested whether arrestin binding requires the G-protein-coupled receptor be a dimer or a multimer. To do this, we encapsulated single-rhodopsin molecules into nanoscale phospholipid particles (so-called nanodiscs) and measured their ability to bind arrestin. Our data clearly show that both visual arrestin and β-arrestin 1 can bind to monomeric rhodopsin and stabilize the active metarhodopsin II form. Interestingly, we find that the monomeric rhodopsin in nanodiscs has a higher affinity for wild-type arrestin binding than does oligomeric rhodopsin in liposomes or nanodiscs, as assessed by stabilization of metarhodopsin II. Together, these results establish that rhodopsin self-association is not required to enable arrestin binding.

Original languageEnglish (US)
Pages (from-to)501-511
Number of pages11
JournalJournal of Molecular Biology
Volume399
Issue number3
DOIs
StatePublished - Jun 2010

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Arrestin
Rhodopsin
G-Protein-Coupled Receptors
Liposomes
Phospholipids

Keywords

  • Arrestin
  • G-protein-coupled receptor
  • Nanodiscs
  • Oligomerization
  • Rhodopsin

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Monomeric rhodopsin is the minimal functional unit required for arrestin binding. / Tsukamoto, Hisao; Sinha, Abhinav; DeWitt, Mark; Farrens, David.

In: Journal of Molecular Biology, Vol. 399, No. 3, 06.2010, p. 501-511.

Research output: Contribution to journalArticle

Tsukamoto, Hisao ; Sinha, Abhinav ; DeWitt, Mark ; Farrens, David. / Monomeric rhodopsin is the minimal functional unit required for arrestin binding. In: Journal of Molecular Biology. 2010 ; Vol. 399, No. 3. pp. 501-511.
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