ArticleAmerican journal of physiology. Renal physiology2008
Human FXYD2 G41R mutation responsible for renal hypomagnesemia behaves as an inward-rectifying cation channel.
Article in American journal of physiology. Renal physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- On the mechanism of hypomagnesemia with treatment-resistant seizures caused by variants of the Na+,K+-ATPase α1 subunit (ATP1A1).The Journal of general physiology · 2026Article
- The functions of FXYD family members in human health and disease.Genes & diseases · 2026Review
- Molecular Basis of Na, K-ATPase Regulation of Diseases: Hormone and FXYD2 Interactions.International journal of molecular sciences · 2024Review
- Navigating the multifaceted intricacies of the NaPhysiological reviews · 2024Review
- Discovery and Characterization of the Phospholemman/SIMP/Viroporin Superfamily.Microbial physiology · 2022Article
- Diseases caused by mutations in the NaAmerican journal of physiology. Cell physiology · 2021Review
- What FXYDs fix.The Journal of general physiology · 2021Article
- FXYD proteins and sodium pump regulatory mechanisms.The Journal of general physiology · 2021Review
- An atlas of human proximal epididymis reveals cell-specific functions and distinct roles for CFTR.Life science alliance · 2020Article
- Identification of a mammalian silicon transporter.American journal of physiology. Cell physiology · 2017Article
- Effect of diaminopropionic acid (Dap) on the biophysical properties of a modified synthetic channel-forming peptide.Molecular pharmaceutics · 2013Article
- Identification of novel tissue-specific genes by analysis of microarray databases: a human and mouse model.PloS one · 2013Article
- Regulation of magnesium balance: lessons learned from human genetic disease.Clinical kidney journal · 2012Article
- A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps.Nature reviews. Molecular cell biology · 2011Review
- A genomic-based approach identifies FXYD domain containing ion transport regulator 2 (FXYD2)gammaa as a pancreatic beta cell-specific biomarker.Diabetologia · 2010Article
- Regulation of magnesium reabsorption in DCT.Pflugers Archiv : European journal of physiology · 2009Review
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Authors and funding
7 authors at 1 institution in 1 country.
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Abstract
A mutation in the human FXYD2 polypeptide (Na-K-ATPase gamma subunit) that changes a conserved transmembrane glycine to arginine is linked to dominant renal hypomagnesemia. Xenopus laevis oocytes injected with wild-type FXYD2 or the mutant G41R cRNAs expressed large nonselective ion currents. However, in contrast to the wild-type FXYD2 currents, inward rectifying cation currents were induced by hyperpolarization pulses in oocytes expressing the G41R mutant. Injection of EDTA into the oocyte removed inward rectification in the oocytes expressing the mutant, but did not alter the nonlinear current-voltage relationship of the wild-type FXYD2 pseudo-steady-state currents. Extracellular divalent ions, Ca2+ and Ba2+, and trivalent cations, La3+, blocked both the wild-type and mutant FXYD2 currents. Site-directed mutagenesis of G41 demonstrated that a positive charge at this site is required for the inward rectification. When the wild-type FXYD2 was expressed in Madin-Darby canine kidney cells, the cells in the presence of a large apical-to-basolateral Mg2+ gradient and at negative potentials had an increase in transepithelial current compared with cells expressing the G41R mutant or control transfected cells. Moreover, this current was inhibited by extracellular Ba2+ at the basolateral surface. These results suggest that FXYD2 can mediate basolateral extrusion of magnesium from cultured renal epithelial cells and provide new insights into the understanding of the possible physiological roles of FXYD2 wild-type and mutant proteins.
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