ArticleThe Journal of biological chemistry2012
β-Subunit of the Ostα-Ostβ organic solute transporter is required not only for heterodimerization and trafficking but also for function.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Altered Bile Acid Transport in Liver Disease.Biomedicines · 2026Review
- Article
- Differential and organ-specific functions of organic solute transporter α and β in experimental cholestasis.JHEP reports : innovation in hepatology · 2022Article
- Physiological Role of Bile Acids Modified by the Gut Microbiome.Microorganisms · 2021Review
- Calsyntenin-3 interacts with the sodium-dependent vitamin C transporter-2 to regulate vitamin C uptake.International journal of biological macromolecules · 2021Article
- Deletion of Intestinal SHP Impairs Short-term Response to Cholic Acid Challenge in Male Mice.Endocrinology · 2021Article
- Modeling Human Bile Acid Transport and Synthesis in Stem Cell-Derived Hepatocytes with a Patient-Specific Mutation.Stem cell reports · 2021Article
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Novel insights into the organic solute transporter alpha/beta, OSTα/β: From the bench to the bedside.Pharmacology & therapeutics · 2020Review
- Regulation of Pain Genes-Capsaicin vs Resiniferatoxin: Reassessment of Transcriptomic Data.Frontiers in pharmacology · 2020Article
- Intestinal Absorption of Bile Acids in Health and Disease.Comprehensive Physiology · 2019Review
- The Biosynthesis, Signaling, and Neurological Functions of Bile Acids.Biomolecules · 2019Review
- Organic solute transporter-β (SLC51B) deficiency in two brothers with congenital diarrhea and features of cholestasis.Hepatology (Baltimore, Md.) · 2018Article
- Characterization of a novel organic solute transporter homologue from Clonorchis sinensis.PLoS neglected tropical diseases · 2018Article
- Article
- The organic solute transporters alpha and beta are induced by hypoxia in human hepatocytes.Liver international : official journal of the International Association for the Study of the Liver · 2015Article
- Clinical application of transcriptional activators of bile salt transporters.Molecular aspects of medicine · 2014Review
- Ostα-/- mice exhibit altered expression of intestinal lipid absorption genes, resistance to age-related weight gain, and modestly improved insulin sensitivity.American journal of physiology. Gastrointestinal and liver physiology · 2014Article
- The Concise Guide to PHARMACOLOGY 2013/14: transporters.British journal of pharmacology · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The organic solute transporter, Ost/Slc51, is composed of two distinct proteins that must heterodimerize to generate transport activity, but the role of the individual subunits in mediating transport activity is unknown. The present study identified regions in Ostβ required for heterodimerization with Ostα, trafficking of the Ostα-Ostβ complex to the plasma membrane, and bile acid transport activity in HEK293 cells. Bimolecular fluorescence complementation analysis revealed that a 25-amino acid peptide containing the Ostβ transmembrane (TM) domain heterodimerized with Ostα, although the resulting complex failed to reach the plasma membrane and generate cellular [(3)H]taurocholate transport activity. Deletion of the single TM domain of Ostβ abolished interaction with Ostα, demonstrating that the TM segment is necessary and sufficient for formation of a heteromeric complex with Ostα. Mutation of the highly conserved tryptophan-asparagine sequence within the TM domain of Ostβ to alanines did not prevent cell surface trafficking, but abolished transport activity. Removal of the N-terminal 27 amino acids of Ostβ resulted in a transporter complex that reached the plasma membrane and exhibited transport activity at 30 °C. Complete deletion of the C terminus of Ostβ abolished [(3)H]taurocholate transport activity, but reinsertion of two native arginines immediately C-terminal to the TM domain rescued this defect. These positively charged residues establish the correct N(exo)/C(cyt) topology of the peptide, in accordance with the positive inside rule. Together, the results demonstrate that Ostβ is required for both proper trafficking of Ostα and formation of the functional transport unit, and identify specific residues of Ostβ critical for these processes.
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