ArticleThe Journal of biological chemistry2015
Disruption of Rhodopsin Dimerization with Synthetic Peptides Targeting an Interaction Interface.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 80 citations in OpenAlex.
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- β2-Adrenergic Receptor Utilizes Distinct Interaction Interfaces to Selectively form Heterooligomers with a Subset of Bitter Taste Receptors.Biochemistry · 2025Article
- Design of Small Non-Peptidic Ligands That Alter Heteromerization between Cannabinoid CBJournal of medicinal chemistry · 2025Article
- Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.PLoS biology · 2025Article
- The double whammy of ER-retention and dominant-negative effects in numerous autosomal dominant diseases: significance in disease mechanisms and therapy.Journal of biomedical science · 2024Review
- Dynamic Dimerization of Chemokine Receptors and Potential Inhibitory Role of Their Truncated Isoforms Revealed through Combinatorial Prediction.International journal of molecular sciences · 2023Article
- Development of tolerance to chemokine receptor antagonists: current paradigms and the need for further investigation.Frontiers in immunology · 2023Review
- Nonretinoid chaperones improve rhodopsin homeostasis in a mouse model of retinitis pigmentosa.JCI insight · 2022Article
- Phospholipid Scrambling by G Protein-Coupled Receptors.Annual review of biophysics · 2022Review
- Disrupting GPCR Complexes with Smart Drug-like Peptides.Pharmaceutics · 2022Review
- Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021Review
- Polyphenols and Visual Health: Potential Effects on Degenerative Retinal Diseases.Molecules (Basel, Switzerland) · 2021Review
- Orally Active Peptide Vector Allows Using Cannabis to Fight Pain While Avoiding Side Effects.Journal of medicinal chemistry · 2021Article
- Unusual mode of dimerization of retinitis pigmentosa-associated F220C rhodopsin.Scientific reports · 2021Article
- Evolutionary Constraint on Visual and Nonvisual Mammalian Opsins.Journal of biological rhythms · 2021Article
- Structure and function of adenosine receptor heteromers.Cellular and molecular life sciences : CMLS · 2021Review
- The F220C and F45L rhodopsin mutations identified in retinitis pigmentosa patients do not cause pathology in mice.Scientific reports · 2020Article
- The Retinoid and Non-Retinoid Ligands of the Rod Visual G Protein-Coupled Receptor.International journal of molecular sciences · 2019Review
- AInternational journal of molecular sciences · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Although homo- and heterodimerizations of G protein-coupled receptors (GPCRs) are well documented, GPCR monomers are able to assemble in different ways, thus causing variations in the interactive interface between receptor monomers among different GPCRs. Moreover, the functional consequences of this phenomenon, which remain to be clarified, could be specific for different GPCRs. Synthetic peptides derived from transmembrane (TM) domains can interact with a full-length GPCR, blocking dimer formation and affecting its function. Here we used peptides corresponding to TM helices of bovine rhodopsin (Rho) to investigate the Rho dimer interface and functional consequences of its disruption. Incubation of Rho with TM1, TM2, TM4, and TM5 peptides in rod outer segment (ROS) membranes shifted the resulting detergent-solubilized protein migration through a gel filtration column toward smaller molecular masses with a reduced propensity for dimer formation in a cross-linking reaction. Binding of these TM peptides to Rho was characterized by both mass spectrometry and a label-free assay from which dissociation constants were calculated. A BRET (bioluminescence resonance energy transfer) assay revealed that the physical interaction between Rho molecules expressed in membranes of living cells was blocked by the same four TM peptides identified in our in vitro experiments. Although disruption of the Rho dimer/oligomer had no effect on the rates of G protein activation, binding of Gt to the activated receptor stabilized the dimer. However, TM peptide-induced disruption of dimer/oligomer decreased receptor stability, suggesting that Rho supramolecular organization could be essential for ROS stabilization and receptor trafficking.
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