ReviewThe Journal of biological chemistry2013
Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase.
Review in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed.
- Structural and functional insights into a ZnNature communications · 2026Article
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- Transcriptional and epigenetic changes associated with lead exposure in spermatozoa.Asian journal of andrology · 2026Article
- Pathophysiological Roles of Two Intracellular P-Type ATPases: The Cancer-Associated NaInternational journal of molecular sciences · 2026Review
- The Landscape of SERCA2 in Cardiovascular Diseases: Expression Regulation, Therapeutic Applications, and Emerging Roles.Biomolecules · 2026Review
- From concept to application: Exploring the evolution and potential of DUBTAC technology.Acta pharmaceutica Sinica. B · 2026Review
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- The SERCA-PLN-DWORF axis in cardiometabolic disease: mechanisms and therapeutic perspectives.Cardiovascular diabetology · 2025Review
- Resistance Exercise Associated with Camu-Camu (Nutrients · 2025Article
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- P-type ATPase magnesium transporter MgtA acts as a dimer.Nature structural & molecular biology · 2025Article
- The endoplasmic reticulum luminal CaPNAS nexus · 2025Article
- The structure and function of P5A-ATPases.Nature communications · 2024Article
- Dephosphorylation and ion binding in prokaryotic calcium transport.Science advances · 2024Article
- Isolation of the Sarcoplasmic Reticulum CaMethods and protocols · 2023Article
- Multiscale computational modeling of the effects of 2'-deoxy-ATP on cardiac muscle calcium handling.Journal of applied physics · 2023Article
- Plastic recognition and electrogenic uniport translocation of 1Chemical science · 2023Article
- Sarcoplasmic Reticulum CaCells · 2023Review
- Structural basis of ion uptake in copper-transporting PNature communications · 2022Article
- Ion Channels, Transporters, and Sensors Interact with the Acidic Tumor Microenvironment to Modify Cancer Progression.Reviews of physiology, biochemistry and pharmacology · 2022Review
12 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) is a transmembrane ion transporter belonging to the P(II)-type ATPase family. It performs the vital task of re-sequestering cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. This minireview focuses on the transport pathways of Ca(2+) and H(+) ions across the lipid bilayer through SERCA. The ion-binding sites of SERCA are accessible from either the cytoplasm or the sarco/endoplasmic reticulum lumen, and the Ca(2+) entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane α-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the C-terminal transmembrane region leading from the ion-binding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca(2+)-free E2 states, suggesting that it may play a functional role in proton release from the ion-binding sites. This is in agreement with molecular dynamics simulations and mutational studies and is in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in P(II)-ATPases including not one, but two cytoplasmic pathways working in concert.
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