ArticleProceedings of the National Academy of Sciences of the United States of America2010
Pore architecture of the ORAI1 store-operated calcium channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.
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Who cites it
94 citing papers in PubMed.
- Mechanistic insights into Orai dynamics during pore opening.Channels (Austin, Tex.) · 2026Review
- Developing Optogenetic Approaches to Study CaCold Spring Harbor perspectives in biology · 2026Review
- STIM-Orai signaling in neurons: integrating calcium dynamics and synaptic plasticity.Cell communication and signaling : CCS · 2026Review
- Is the SPLUNC1-Orai1 axis a critical determinant of lung health?Biochemical Society transactions · 2025Review
- ORAI CaBiomolecules · 2024Review
- Universal CAR 2.0 to overcome current limitations in CAR therapy.Frontiers in immunology · 2024Review
- Extracellular calcium functions as a molecular glue for transmembrane helices to activate the scramblase Xkr4.Nature communications · 2023Article
- Regulatory mechanisms controlling store-operated calcium entry.Frontiers in physiology · 2023Review
- CRAC and SK Channels: Their Molecular Mechanisms Associated with Cancer Cell Development.Cancers · 2022Review
- Review
- The Role of Lipids in CRAC Channel Function.Biomolecules · 2022Review
- Alteration of STIM1/Orai1-Mediated SOCE in Skeletal Muscle: Impact in Genetic Muscle Diseases and Beyond.Cells · 2021Review
- Isoform-Specific Properties of Orai Homologues in Activation, Downstream Signaling, Physiology and Pathophysiology.International journal of molecular sciences · 2021Review
- Novel ORAI1 Mutation Disrupts Channel Trafficking Resulting in Combined Immunodeficiency.Journal of clinical immunology · 2021Article
- An open pore structure of the Orai channel, finally.Cell calcium · 2021Article
- The Orai Pore Opening Mechanism.International journal of molecular sciences · 2021Review
- Interrogating permeation and gating of Orai channels using chemical modification of cysteine residues.Methods in enzymology · 2021Article
- The Impact of Mutation L138F/L210F on the Orai Channel: A Molecular Dynamics Simulation Study.Frontiers in molecular biosciences · 2021Article
- Synthesis and Characterization of Store-Operated Calcium Entry Inhibitors Active in the Submicromolar Range.International journal of molecular sciences · 2020Article
- Molecular Choreography and Structure of CaMembranes · 2020Review
34 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
ORAI1 is the pore-forming subunit of the calcium release-activated calcium (CRAC) channel, a store-operated channel that is central to Ca(2+) signaling in mammalian cells. Electrophysiological data have shown that the acidic residues E106 in transmembrane helix 1 (TM1) and E190 in TM3 contribute to the high selectivity of ORAI1 channels for Ca(2+). We have examined the pore architecture of the ORAI1 channel using ORAI1 proteins engineered to contain either one or two cysteine residues. Disulfide cross-linking shows that ORAI1 assembles as a tetramer or a higher oligomer with TM1 centrally located. Cysteine side chains projecting from TM1 at position 88, 95, 102, or 106 cross-link efficiently to the corresponding side chain in a second ORAI1 monomer. Cysteine residues at position 190 or at surrounding positions in TM3 do not cross-link. We conclude that E106 residues in wild-type ORAI1 are positioned to form a Ca(2+) binding site in the channel pore and that E190 interacts less directly with ions traversing the pore. The cross-linking data further identify a relatively rigid segment of TM1 adjacent to E106 that is likely to contribute to the selectivity filter.
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