Residues Contributing to the Ca2+ and K+ Binding Pocket of the NCKX2 Na+/Ca2+-K+ Exchanger
Open accessAbstract
The Na(+)/Ca(2+)-K(+) exchanger (NCKX) extrudes Ca(2+) from cells utilizing both the inward Na(+) gradient and the outward K(+) gradient. NCKX is thought to operate by a consecutive mechanism in which a cation binding pocket accommodates both Ca(2+) and K(+) and alternates between inward and outward facing conformations. Here we developed a simple fluorometric method to analyze changes in K(+) and Ca(2+) dependences of mutant NCKX2 proteins in which candidate residues within membrane-spanning domains were substituted. The largest shifts in both K(+) and Ca(2+) dependences compared with wild-type NCKX2 were observed for the charge-conservative substitutions of Glu(188) and Asp(548), whereas the size-conservative substitutions resulted in nonfunctional proteins. Substitution of several other residues including two proline residues (Pro(187) and Pro(547)), three additional acidic residues (Asp(258), Glu(265), Glu(533)), and two hydroxyl-containing residues (Ser(185) and Ser(545)) showed smaller shifts, but shifts in Ca(2+) dependence were invariably accompanied by shifts in K(+) dependence. We conclude that Glu(188) and Asp(548) are the central residues of a single cation binding pocket that can accommodate both K(+) and Ca(2+). Furthermore, a single set of residues lines a transport pathway for both K(+) and Ca(2+).
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The region containing the polymorphic residue of NCKX5 contains a number of residues that are critical for exchange function.
“This region contains a number of residues that are critical for exchange function (14 -16), and the experimentally determined topology for NCKX2 suggests that the polymorphic residue of NCKX5 sits in a transmembrane domain (17).”
From SLC24A5 encodes a trans-Golgi network protein with potassium-dependent sodium-calcium exchange activity that regulates human epidermal melanogenesis (2008) · cites this paper as [15]
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- Authors
- Kang, K.-J., Kinjo, T. G., Szerencsei, R. T., & Schnetkamp, P. P. M.
- Affiliations
- University of Calgary (CA)
- Corresponding author
- Schnetkamp, Paul P.M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-02
- Volume
- 280
- Issue
- 8
- Pages
- 6823-6833
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1995441828
- Cited by
- 44
- References
- 32
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 1 · 2020: 1 · 2019: 1 · 2018: 3 · 2017: 3 · 2016: 2 · 2015: 1 · 2014: 2 · 2013: 6 · 2012: 2
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Foundation Fighting Blindness
- Fondation pour la Recherche Médicale
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- NCKX2, calcium binding, potassium binding, proline residues, acidic residues, site-directed mutagenesis, fluorometric assay, transport pathways
- MeSH terms
- Amino Acids, Animals, Binding Sites, Biological Transport, Calcium, Cell Line, Fluorometry, Humans, Insecta, Kinetics, Potassium, Sodium-Calcium Exchanger, Amino Acid Substitution, Static Electricity
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