ArticleBiochimica et biophysica acta. Molecular basis of disease2018
Misfolded rhodopsin mutants display variable aggregation properties.
Article in Biochimica et biophysica acta. Molecular basis of disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Aggregation of the Constitutively Active K296E Rhodopsin Mutant Contributes to Retinal Degeneration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- A Y178C rhodopsin mutation causes aggregation and comparatively severe retinal degeneration.Cell death discovery · 2025Article
- Mutant dominant-negativeFrontiers in molecular biosciences · 2024Article
- Rhodopsin-associated retinal dystrophy: Disease mechanisms and therapeutic strategies.Frontiers in neuroscience · 2023Review
- Nonretinoid chaperones improve rhodopsin homeostasis in a mouse model of retinitis pigmentosa.JCI insight · 2022Article
- Article
- Misfolded G Protein-Coupled Receptors and Endocrine Disease. Molecular Mechanisms and Therapeutic Prospects.International journal of molecular sciences · 2021Review
- Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021Review
- Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021Review
- Co-delivery of glial cell-derived neurotrophic factor (GDNF) and tauroursodeoxycholic acid (TUDCA) from PLGA microspheres: potential combination therapy for retinal diseases.Drug delivery and translational research · 2021Article
- Differential Aggregation Properties of Mutant Human and Bovine Rhodopsin.Biochemistry · 2021Article
- Structure network-based landscape of rhodopsin misfolding by mutations and algorithmic prediction of small chaperone action.Computational and structural biotechnology journal · 2021Article
- Retinal degeneration in mice expressing the constitutively active G90D rhodopsin mutant.Human molecular genetics · 2020Article
- The Retinoid and Non-Retinoid Ligands of the Rod Visual G Protein-Coupled Receptor.International journal of molecular sciences · 2019Review
- Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019Review
- Flavonoids enhance rod opsin stability, folding, and self-association by directly binding to ligand-free opsin and modulating its conformation.The Journal of biological chemistry · 2019Article
- Detection of misfolded rhodopsin aggregates in cells by Förster resonance energy transfer.Methods in cell biology · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The largest class of rhodopsin mutations causing autosomal dominant retinitis pigmentosa (adRP) is mutations that lead to misfolding and aggregation of the receptor. The misfolding mutants have been characterized biochemically, and categorized as either partial or complete misfolding mutants. This classification is incomplete and does not provide sufficient information to fully understand the disease pathogenesis and evaluate therapeutic strategies. A Förster resonance energy transfer (FRET) method was utilized to directly assess the aggregation properties of misfolding rhodopsin mutants within the cell. Partial (P23H and P267L) and complete (G188R, H211P, and P267R) misfolding mutants were characterized to reveal variability in aggregation properties. The complete misfolding mutants all behaved similarly, forming aggregates when expressed alone, minimally interacting with the wild-type receptor when coexpressed, and were unresponsive to treatment with the pharmacological chaperone 9-cis retinal. In contrast, variability was observed between the partial misfolding mutants. In the opsin form, the P23H mutant behaved similarly as the complete misfolding mutants. In contrast, the opsin form of the P267L mutant existed as both aggregates and oligomers when expressed alone and formed mostly oligomers with the wild-type receptor when coexpressed. The partial misfolding mutants both reacted similarly to the pharmacological chaperone 9-cis retinal, displaying improved folding and oligomerization when expressed alone but aggregating with wild-type receptor when coexpressed. The observed differences in aggregation properties and effect of 9-cis retinal predict different outcomes in disease pathophysiology and suggest that retinoid-based chaperones will be ineffective or even detrimental.
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