2016
DOI: 10.1042/bcj20160422
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Quaternary structures of opsin in live cells revealed by FRET spectrometry

Abstract: Rhodopsin is a prototypical G-protein coupled receptor (GPCR) that initiates phototransduction in the retina. The receptor consists of the apoprotein opsin covalently linked to the inverse agonist 11-cis retinal. Rhodopsin and opsin have been shown to form oligomers within the outer segment disc membranes of rod photoreceptor cells. However, the physiological relevance of the observed oligomers has been questioned since observations were made on samples prepared from the retina at low temperatures. To investig… Show more

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Cited by 50 publications
(64 citation statements)
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References 82 publications
(116 reference statements)
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“…Consistent with these findings, a subsequent Förster resonance energy transfer study confirmed the concentration-dependent oligomerization of rhodopsin in the membrane and showed that rhodopsin exists in multiple oligomeric forms dictated by its concentration and the equilibrium constants that define the formation of each oligomeric form [76]. We show here that computing the mean or median nanodomain size can be misleading because of the skewed distribution of values.…”
Section: Discussionsupporting
confidence: 74%
See 1 more Smart Citation
“…Consistent with these findings, a subsequent Förster resonance energy transfer study confirmed the concentration-dependent oligomerization of rhodopsin in the membrane and showed that rhodopsin exists in multiple oligomeric forms dictated by its concentration and the equilibrium constants that define the formation of each oligomeric form [76]. We show here that computing the mean or median nanodomain size can be misleading because of the skewed distribution of values.…”
Section: Discussionsupporting
confidence: 74%
“…In accord with the scheme previously reported for rhodopsin oligomerization [76], changes in the distribution of nanodomains or oligomeric forms of rhodopsin can arise from changes in rhodopsin concentration or equilibrium constants. The differences observed in the distribution of rhodopsin nanodomain sizes in mice housed in cyclic lighting, 10 days constant dark or 10 days constant light conditions can be explained by differences in rhodopsin concentration alone.…”
Section: Discussionsupporting
confidence: 68%
“…The β1‐adrenergic receptor (B1AR) exists predominantly as a monomer at the plasma membrane and the closely related β2‐adrenergic receptor splits its time roughly equally between monomeric and dimeric states . Receptor oligomerization is highly dynamic at physiological concentrations of receptor, as demonstrated by recent studies with the neurotensin receptor NTSR1 and rhodopsin . Changes in diffusion rate may serve to change receptor‐effector coupling, and GPCR‐G protein complexes appear to diffuse much more rapidly than GPCRs alone …”
Section: Basal Receptor Localization and Agonist‐dependent Redistribumentioning
confidence: 99%
“…In order to localize mEGFP to the plasma membrane a palmitoylation-myristolation (P-M) sequence was added to the amino terminal of the fluorescent protein, as in refs 27 and 42. hD 3 R-mEGFP construct was made by subcloning PCR amplified hD 3 R between the KpnI and SmaI sites of pEGFPN-1 plasmid (Takara Bio Europe/Clontech, Saint-Germain-en-Laye, France).…”
Section: Experimental Proceeduresmentioning
confidence: 99%