ArticleThe Journal of biological chemistry2008
Conserved aspartic acid residues lining the extracellular loop 1 of sodium-coupled bile acid transporter ASBT Interact with Na+ and 7alpha-OH moieties on the ligand cholestane skeleton.
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 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Structural insight into sodium-dependent bile acid transport by members of the SLC10 family.Structure (London, England : 1993) · 2026Article
- Article
- Intestinal Absorption of Bile Acids in Health and Disease.Comprehensive Physiology · 2019Review
- Mechanistic interpretation of conventional Michaelis-Menten parameters in a transporter system.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2014Article
- Structural requirements of the human sodium-dependent bile acid transporter (hASBT): role of 3- and 7-OH moieties on binding and translocation of bile acids.Molecular pharmaceutics · 2014Article
- Transmembrane domain II of the human bile acid transporter SLC10A2 coordinates sodium translocation.The Journal of biological chemistry · 2013Article
- Transmembrane domain V plays a stabilizing role in the function of human bile acid transporter SLC10A2.Biochemistry · 2013Article
- Article
- Transmembrane helix 1 contributes to substrate translocation and protein stability of bile acid transporter SLC10A2.The Journal of biological chemistry · 2011Article
- The cytosolic half of helix III forms the substrate exit route during permeation events of the sodium/bile acid cotransporter ASBT.Biochemistry · 2009Article
- The solute carrier family 10 (SLC10): beyond bile acid transport.Molecular aspects of medicineReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Functional contributions of residues Val-99-Ser-126 lining extracellular loop (EL) 1 of the apical sodium-dependent bile acid transporter were determined via cysteine-scanning mutagenesis, thiol modification, and in silico interpretation. Despite membrane expression for all but three constructs (S112C, Y117C, S126C), most EL1 mutants (64%) were inactivated by cysteine mutation, suggesting a functional role during sodium/bile acid co-transport. A negative charge at conserved residues Asp-120 and Asp-122 is required for transport function, whereas neutralization of charge at Asp-124 yields a functionally active transporter. D124A exerts low affinity for common bile acids except deoxycholic acid, which uniquely lacks a 7alpha-hydroxyl (OH) group. Overall, we conclude that (i) Asp-122 functions as a Na(+) sensor, binding one of two co-transported Na(+) ions, (ii) Asp-124 interacts with 7alpha-OH groups of bile acids, and (iii) apolar EL1 residues map to hydrophobic ligand pharmacophore features. Based on these data, we propose a comprehensive mechanistic model involving dynamic salt bridge pairs and hydrogen bonding involving multiple residues to describe sodium-dependent bile acid transporter-mediated bile acid and cation translocation.
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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.