ArticleThe Journal of biological chemistry2009
NBCe1-A Transmembrane Segment 1 Lines the Ion Translocation Pathway.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Molecular dynamics simulations of lipid-protein interactions in SLC4 proteins.Biophysical journal · 2024Article
- The role of NaPflugers Archiv : European journal of physiology · 2024Review
- Lack of Charge Interaction in the Ion Binding Site Determines Anion Selectivity in the Sodium Bicarbonate Cotransporter NBCe1.International journal of molecular sciences · 2022Article
- Article
- CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1.Nature communications · 2018Article
- Interplay between disulfide bonding and N-glycosylation defines SLC4 Na+-coupled transporter extracellular topography.The Journal of biological chemistry · 2015Article
- Structure and Function of SLC4 Family [Formula: see text] Transporters.Frontiers in physiology · 2015Article
- 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
- SLC4A11 is an EIPA-sensitive Na(+) permeable pHi regulator.American journal of physiology. Cell 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
- The divergence, actions, roles, and relatives of sodium-coupled bicarbonate transporters.Physiological reviews · 2013Review
- Topology of NBCe1 protein transmembrane segment 1 and structural effect of proximal renal tubular acidosis (pRTA) S427L mutation.The Journal of biological chemistry · 2013Article
- SLC4A transporters.Current topics in membranes · 2012Article
- Differential roles of cysteine residues in the cellular trafficking, dimerization, and function of the high-density lipoprotein receptor, SR-BI.Biochemistry · 2011Article
- Structural and functional characterization of the C-terminal transmembrane region of NBCe1-A.The Journal of biological chemistry · 2010Article
- Topological location and structural importance of the NBCe1-A residues mutated in proximal renal tubular acidosis.The Journal of biological chemistry · 2010Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The electrogenic Na(+)/HCO(3)(-) cotransporter (NBCe1-A) transports sodium and bicarbonate across the basolateral membrane of the renal proximal tubule. In this study the structural requirement of transmembrane segment 1 (TM1) residues in mediating NBCe1-A transport was investigated. Twenty-five introduced cysteine mutants at positions Gln-424 to Gly-448 were tested for their sensitivity to the methanethiosulfonate reagents (2-sulfonatoethyl) methanethiosulfonate (MTSES), [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET), and (2-aminoethyl) methanethiosulfonate (MTSEA). Two mutants, T442C and A435C, showed 100 and 70% sensitivity, respectively, to inhibition by all the three methanethiosulfonate (MTS) reagents, I441C had >50% sensitivity to MTSET and MTSEA, and A428C had 50% sensitivity to MTSEA inhibition. A helical wheel plot showed that mutants T442C, A435C, and A428C are clustered on one face of TM1 within a 100 degrees arc. Topology analysis of TM1 with biotin maleimide and 2-((5(6)-tetramethylrhodamine)carboxylamino) ethyl methanethiosulfonate (MTS-TAMRA) revealed Thr-442 marks the C-terminal end of TM1 and that extracellular FGGLLG stretch is in a small aqueous-accessible cavity. Functional studies indicated that Thr-442 resides in a narrow region of the ion translocation pore with strong delta(-) helical dipole influence. Analysis of the corresponding residue of NBCe1-A-Thr-442 in AE1 (Thr-422) shows it is functionally insensitive to MTSES and unlabeled with MTS-TAMRA, indicating that AE1-TM1 is oriented differently from NBCe1-A. In summary, we have identified residues Thr-442, Ala-435, and Ala-428 in TM1 lining the ion translocation pore of NBCe1-A. Our findings are suggestive of a delta(-) helical dipole at the C-terminal end of TM1 involving Thr-442 that plays a critical role in the function of the cotransporter.
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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.