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• W2087973190 abstract "Na+/Ca2+-K+ exchangers (NCKX; gene family SLC24) are plasma membrane Ca2+ transporters that mediate the extrusion of one Ca2+ ion and one K+ ion in exchange for four Na+ ions. NCKX is modeled to have two sets of five transmembrane segments separated by a large cytosolic loop; within each set of transmembrane segments are regions of internal symmetry termed α1 and α2 repeats. The central residues that are important for Ca2+ and K+ liganding and transport have been identified in NCKX2, and they comprise three central acidic residues, Glu188 in α1 and Asp548 and Asp575 in α2, as well as Ser/Thr residues one-helical turn away from these residues. In this study, we have scanned through more than 100 single-residue substitutions of NCKX2 for shifts in Na+ affinity using a fluorescence assay to monitor changes in free Ca2+ in HEK293 cells treated with gramicidin to control intracellular Na+. We have identified 31 residues that, when substituted, result in shifts in Na+ affinity, either toward higher or lower Km values when compared with wild type NCKX2 (Km for Na+ 58 mm). These residues include the central acidic residues Glu188, Asp548, and Asp575, and their neighboring residues in α1 and α2, in addition to a number of newly investigated residues in transmembrane segment 3. Our results relate the identification of residues important for Na+ transport in this study to those previously identified as important in the counter-transport of Ca2+ and K+, lending support to the alternating access model of transmembrane transport. Na+/Ca2+-K+ exchangers (NCKX; gene family SLC24) are plasma membrane Ca2+ transporters that mediate the extrusion of one Ca2+ ion and one K+ ion in exchange for four Na+ ions. NCKX is modeled to have two sets of five transmembrane segments separated by a large cytosolic loop; within each set of transmembrane segments are regions of internal symmetry termed α1 and α2 repeats. The central residues that are important for Ca2+ and K+ liganding and transport have been identified in NCKX2, and they comprise three central acidic residues, Glu188 in α1 and Asp548 and Asp575 in α2, as well as Ser/Thr residues one-helical turn away from these residues. In this study, we have scanned through more than 100 single-residue substitutions of NCKX2 for shifts in Na+ affinity using a fluorescence assay to monitor changes in free Ca2+ in HEK293 cells treated with gramicidin to control intracellular Na+. We have identified 31 residues that, when substituted, result in shifts in Na+ affinity, either toward higher or lower Km values when compared with wild type NCKX2 (Km for Na+ 58 mm). These residues include the central acidic residues Glu188, Asp548, and Asp575, and their neighboring residues in α1 and α2, in addition to a number of newly investigated residues in transmembrane segment 3. Our results relate the identification of residues important for Na+ transport in this study to those previously identified as important in the counter-transport of Ca2+ and K+, lending support to the alternating access model of transmembrane transport." @default.
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• W2087973190 date "2010-05-01" @default.
• W2087973190 modified "2023-10-16" @default.
• W2087973190 title "Residues Contributing to the Na+-binding Pocket of the SLC24 Na+/Ca2+-K+ Exchanger NCKX2" @default.
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• W2087973190 doi "https://doi.org/10.1074/jbc.m109.090738" @default.
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