ArticlePloS one2013
Vitamin A transport and the transmembrane pore in the cell-surface receptor for plasma retinol binding protein.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Vitamin A attenuates PFOS-induced neurotoxicity and alters early proximity patterns to conspecifics in zebrafish larvae.Frontiers in behavioral neuroscience · 2025Article
- Effects of one-week intake of different edible oils on the urinary proteome of rats.Frontiers in nutrition · 2025Article
- The role of SLC transporters for brain health and disease.Cellular and molecular life sciences : CMLS · 2021Review
- Regulatory mechanism for the transmembrane receptor that mediates bidirectional vitamin A transport.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Electronegative low-density lipoprotein of patients with metabolic syndrome induces pathogenesis of aorta through disruption of the stimulated by retinoic acid 6 cascade.Journal of diabetes investigation · 2020Article
- Simultaneous Determination of Protein Structure and Dynamics Using Cryo-Electron Microscopy.Biophysical journal · 2018Article
- Diet-dependent retinoid effects on liver gene expression include stellate and inflammation markers and parallel effects of the nuclear repressor Shp.The Journal of nutritional biochemistry · 2017Article
- Structure of the STRA6 receptor for retinol uptake.Science (New York, N.Y.) · 2016Article
- Electronegative low density lipoprotein induces renal apoptosis and fibrosis: STRA6 signaling involved.Journal of lipid research · 2016Article
- Genome-wide transcriptome analysis of hypothalamus in rats with inherited stress-induced arterial hypertension.BMC genetics · 2016Article
- Retinol-binding protein-4 and hs-CRP levels in patients with migraine.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2015Article
- Vitamin A Transport Mechanism of the Multitransmembrane Cell-Surface Receptor STRA6.Membranes · 2015Review
- STRA6: role in cellular retinol uptake and efflux.Hepatobiliary surgery and nutrition · 2015Review
- An alternative retinoic acid-responsive Stra6 promoter regulated in response to retinol deficiency.The Journal of biological chemistry · 2015Article
- Crossing the barrier: STRA6 in epidermal differentiation.The Journal of investigative dermatology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Vitamin A and its derivatives (retinoids) play diverse and crucial functions from embryogenesis to adulthood and are used as therapeutic agents in human medicine for eye and skin diseases, infections and cancer. Plasma retinol binding protein (RBP) is the principal and specific vitamin A carrier in the blood and binds vitamin A at 1:1 ratio. STRA6 is the high-affinity membrane receptor for RBP and mediates cellular vitamin A uptake. STRA6 null mice have severely depleted vitamin A reserves for vision and consequently have vision loss, even under vitamin A sufficient conditions. STRA6 null humans have a wide range of severe pathological phenotypes in many organs including the eye, brain, heart and lung. Known membrane transport mechanisms involve transmembrane pores that regulate the transport of the substrate (e.g., the gating of ion channels). STRA6 represents a new type of membrane receptor. How this receptor interacts with its transport substrate vitamin A and the functions of its nine transmembrane domains are still completely unknown. These questions are critical to understanding the molecular basis of STRA6's activities and its regulation. We employ acute chemical modification to introduce chemical side chains to STRA6 in a site-specific manner. We found that modifications with specific chemicals at specific positions in or near the transmembrane domains of this receptor can almost completely suppress its vitamin A transport activity. These experiments provide the first evidence for the existence of a transmembrane pore, analogous to the pore of ion channels, for this new type of cell-surface receptor.
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