ArticleThe Journal of general physiology2016
Electrophysiological characterization of the archaeal transporter NCX_Mj using solid supported membrane technology.
Article in The Journal of general physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 17 citations in OpenAlex.
- Investigating the Effect of Membrane Composition on the Selective Ammonium Transport of Escherichia coli AmtB Membrane Proteins.ACS applied engineering materials · 2025Article
- Conformational free-energy landscapes of a NaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Transport of metformin metabolites by guanidinium exporters of the small multidrug resistance family.The Journal of general physiology · 2024Article
- An Overview of Cell-Based Assay Platforms for the Solute Carrier Family of Transporters.Frontiers in pharmacology · 2021Review
- Protein Adsorption on Solid Supported Membranes: Monitoring the Transport Activity of P-Type ATPases.Molecules (Basel, Switzerland) · 2020Review
- Functional Characterization of SLC Transporters Using Solid Supported Membranes.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Functional Reconstitution of Membrane Proteins Derived From Eukaryotic Cell-Free Systems.Frontiers in pharmacology · 2019Article
- Carriers, exchangers, and cotransporters in the first 100 years of theThe Journal of general physiology · 2018Review
- The prokaryotic NaThe Journal of general physiology · 2018Article
- Discovery of Compounds that Positively Modulate the High Affinity Choline Transporter.Frontiers in molecular neuroscience · 2017Article
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sodium-calcium exchangers (NCXs) are membrane transporters that play an important role in Ca(2+) homeostasis and Ca(2+) signaling. The recent crystal structure of NCX_Mj, a member of the NCX family from the archaebacterium Methanococcus jannaschii, provided insight into the atomistic details of sodium-calcium exchange. Here, we extend these findings by providing detailed functional data on purified NCX_Mj using solid supported membrane (SSM)-based electrophysiology, a powerful but unexploited tool for functional studies of electrogenic transporter proteins. We show that NCX_Mj is highly selective for Na(+), whereas Ca(2+) can be replaced by Mg(2+) and Sr(2+) and that NCX_Mj can be inhibited by divalent ions, particularly Cd(2+) By directly comparing the apparent affinities of Na(+) and Ca(2+) for NCX_Mj with those for human NCX1, we show excellent agreement, indicating a strong functional similarity between NCX_Mj and its eukaryotic isoforms. We also provide detailed instructions to facilitate the adaption of this method to other electrogenic transporter proteins. Our findings demonstrate that NCX_Mj can serve as a model for the NCX family and highlight several possible applications for SSM-based electrophysiology.
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