ArticleThe Journal of biological chemistry2010
Topological location and structural importance of the NBCe1-A residues mutated in proximal renal tubular acidosis.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
- Molecular determinants of [Formula: see text] and cation transport in the human cation-dependent ClAmerican journal of physiology. Cell physiology · 2025Article
- The role of NaPflugers Archiv : European journal of physiology · 2024Review
- Genetic Diagnosis and Treatment of Inherited Renal Tubular Acidosis.Kidney diseases (Basel, Switzerland) · 2023Review
- A guide to plasma membrane solute carrier proteins.The FEBS journal · 2021Review
- The role of disease-linked residue glutamine-913 in support of the structure and function of the human electrogenic sodium/bicarbonate cotransporter NBCe1-A.Scientific reports · 2018Article
- NBCe1 expression is required for normal renal ammonia metabolism.American journal of physiology. Renal physiology · 2015Article
- Rescue of the temperature-sensitive, autosomal-recessive mutation R298S in the sodium-bicarbonate cotransporter NBCe1-A characterized by a weakened dimer and abnormal aggregation.Biochimica et biophysica acta · 2015Article
- Therapeutic effect of prenatal alkalization and PTC124 in Na(+)/HCO3(-) cotransporter 1 p.W516* knock-in mice.Gene therapy · 2015Article
- Interplay between disulfide bonding and N-glycosylation defines SLC4 Na+-coupled transporter extracellular topography.The Journal of biological chemistry · 2015Article
- Regulators of Slc4 bicarbonate transporter activity.Frontiers in physiology · 2015Review
- Structure and Function of SLC4 Family [Formula: see text] Transporters.Frontiers in physiology · 2015Article
- Molecular mechanisms and regulation of urinary acidification.Comprehensive Physiology · 2014Review
- Cation-coupled bicarbonate transporters.Comprehensive Physiology · 2014Review
- NBCe1 as a model carrier for understanding the structure-function properties of Na⁺ -coupled SLC4 transporters in health and disease.Pflugers Archiv : European journal of physiology · 2014Review
- Proximal renal tubular acidosis mediated by mutations in NBCe1-A: unraveling the transporter's structure-functional properties.Frontiers in physiology · 2013Review
- Molecular mechanisms of renal and extrarenal manifestations caused by inactivation of the electrogenic Na(+)-HCO3 (-) cotransporter NBCe1.Frontiers in physiology · 2013Review
- Identification of dominant negative effect of L522P mutation in the electrogenic Na⁺-HCO₃⁻ cotransporter NBCe1.Pflugers Archiv : European journal of physiology · 2013Article
- Structure, function, and regulation of the SLC4 NBCe1 transporter and its role in causing proximal renal tubular acidosis.Current opinion in nephrology and hypertension · 2013Review
- Missense mutation T485S alters NBCe1-A electrogenicity causing proximal renal tubular acidosis.American journal of physiology. Cell physiology · 2013Article
- Substitution of transmembrane domain Cys residues alters pH(o)-sensitive anion transport by AE2/SLC4A2 anion exchanger.Pflugers Archiv : European journal of physiology · 2013Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
NBCe1-A electrogenically cotransports Na(+) and HCO(3)(-) across the basolateral membrane of renal proximal tubule cells. Eight missense mutations and 3 nonsense mutations in NBCe1-A cause severe proximal renal tubular acidosis (pRTA). In this study, the topologic properties and structural importance of the 8 endogenous residues mutated in pRTA and the in situ topology of NBCe1-A were examined by the substituted cysteine accessibility method. Of the 55 analyzed individually introduced cysteines, 8 were labeled with both membrane permeant (biotin maleimide (BM)) and impermeant (2-((5(6)-tetramethylrhodamine)carboxylamino)ethyl methanethiosulfonate (MTS-TAMRA)) sulfhydryl reagents, 4 with only BM, and 3 with only MTS-TAMRA. The location of the labeled and unlabeled introduced cysteines clearly indicates that the transmembrane region of NBCe1-A contains 14 transmembrane segments (TMs). In this in situ based NBCe1-A topology, residues mutated in pRTA (pRTA residues) are assigned as: Ser(427), TM1; Thr(485) and Gly(486), TM3; Arg(510) and Leu(522), TM4; Ala(799), TM10; and Arg(881), TM12. Substitution of pRTA residues with cysteines impaired the membrane trafficking of R510C and R881C, the remaining membrane-processed constructs had various impaired transport function. Surprisingly, none of the membrane-processed constructs was accessible to labeling with BM and MTS-TAMRA, nor were they functionally sensitive to the inhibition by (2-aminoethyl)methanethiosulfonate. Functional analysis of Thr(485) with different amino acid substitutions indicated it resides in a unique region important for NBCe1-A function. Our findings demonstrate that the pRTA residues in NBCe1-A are buried in the protein complex/lipid bilayer where they perform important structural roles.
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