ArticleThe Journal of biological chemistry2008
An essential ligand-binding domain in the membrane receptor for retinol-binding protein revealed by large-scale mutagenesis and a human polymorphism.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 71 citations in OpenAlex.
- Advances and therapeutic opportunities in visual cycle modulation.Progress in retinal and eye research · 2025Review
- Loss of the vitamin A receptor RBPR2 in mice disrupts whole-body retinoid homeostasis and the quantitative balance regulating retinylidene protein synthesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- The Effects of STRA6 Regulation of the Circadian Rhythm on Choroidal Neovascularization.Investigative ophthalmology & visual science · 2024Article
- Article
- Correlation between the Serum Concentration of Vitamin A and Disease Severity in Patients Carrying p.G90D inInternational journal of molecular sciences · 2023Article
- Mapping of the extracellular RBP4 ligand binding domain on the RBPR2 receptor for Vitamin A transport.Frontiers in cell and developmental biology · 2023Article
- Mice Lacking the Systemic Vitamin A Receptor RBPR2 Show Decreased Ocular Retinoids and Loss of Visual Function.Nutrients · 2022Article
- Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease.Nutrients · 2022Review
- The Role of Vitamin A in Retinal Diseases.International journal of molecular sciences · 2022Review
- A master of all trades - linking retinoids to different signalling pathways through the multi-purpose receptor STRA6.Cell death discovery · 2021Review
- Physiologically Relevant Free CaJournal of molecular biology · 2021Article
- Biological Functions of RBP4 and Its Relevance for Human Diseases.Frontiers in physiology · 2021Review
- The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Article
- STRA6 Polymorphisms Are Associated With EGFR Mutations in Locally-Advanced and Metastatic Non-Small Cell Lung Cancer Patients.Frontiers in oncology · 2020Article
- Sample preparation for structural and functional analyses of the STRA6 receptor for retinol-binding protein.Methods in enzymology · 2020Article
- Genetic architecture of retinoic-acid signaling-associated ocular developmental defects.Human genetics · 2019Review
- Structural biology of 11-The Biochemical journal · 2018Review
- Molecular Basis for Vitamin A Uptake and Storage in Vertebrates.Nutrients · 2016Review
- Retinoids and Retinal Diseases.Annual review of vision science · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Plasma retinol-binding protein (RBP), the principal carrier of vitamin A in the blood, delivers vitamin A from liver, the site of storage, to distant organs that need vitamin A, such as the eye, brain, placenta, and testis. STRA6 is a high-affinity membrane receptor for RBP and mediates vitamin A uptake in these target organs. STRA6 is a 74-kDa multi-transmembrane domain protein that represents a new class of membrane transport protein. In this study, we used an unbiased strategy by analyzing >900 random mutants of STRA6 to study its structure and function, and we identified an essential RBP-binding domain in STRA6. Mutations in any of the three essential residues in this domain can almost completely abolish binding of STRA6 to RBP and its vitamin A uptake activity from holo-RBP without affecting its cell surface expression. We have also functionally characterized the mutations in human STRA6 that cause severe birth defects as well as several human polymorphisms. All STRA6 mutants associated with severe birth defects have largely abolished vitamin A uptake activity, consistent with the severe clinical phenotypes. In addition, we have identified a human polymorphism that significantly reduces the vitamin A uptake activity of STRA6. Interestingly, the residue affected by this polymorphism is located in the RBP-binding domain we identified, and the polymorphism causes decreased vitamin A uptake by reducing RBP binding. This study identifies an essential functional domain in STRA6 and a human polymorphism in this domain that leads to reduced vitamin A uptake activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.