ArticleProceedings of the National Academy of Sciences of the United States of America2008
The RCK2 domain of the human BKCa channel is a calcium sensor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Article
- Cytochrome C-like Domain Within the Human BK Channel.International journal of molecular sciences · 2025Article
- Transmembrane determinants of voltage-gating differences between BK (Slo1) and Slo3 channels.Biophysical journal · 2024Article
- Structural mapping of patient-associated KCNMA1 gene variants.Biophysical journal · 2024Article
- BK Channelopathies andAnnual review of physiology · 2024Review
- External Hemin as an Inhibitor of Mitochondrial Large-Conductance Calcium-Activated Potassium Channel Activity.International journal of molecular sciences · 2022Article
- Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021Review
- BK Channel Gating Mechanisms: Progresses Toward a Better Understanding of Variants Linked Neurological Diseases.Frontiers in physiology · 2021Review
- A Calcium Sensor Discovered in Bluetongue Virus Nonstructural Protein 2 Is Critical for Virus Replication.Journal of virology · 2020Article
- FeACS chemical biology · 2020Article
- From Local to Global Modeling for Characterizing Calcium Dynamics and Their Effects on Electrical Activity and Exocytosis in Excitable Cells.International journal of molecular sciences · 2019Article
- Article
- RIM-binding proteins recruit BK-channels to presynaptic release sites adjacent to voltage-gated CaThe EMBO journal · 2018Article
- Molecular determinants of CaScientific reports · 2018Article
- Physiological Roles and Therapeutic Potential of CaFrontiers in molecular neuroscience · 2018Review
- Identification of a Novel EF-Loop in the N-terminus of TRPM2 Channel Involved in Calcium Sensitivity.Frontiers in pharmacology · 2018Article
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- Modulation of BK Channel Function by Auxiliary Beta and Gamma Subunits.International review of neurobiology · 2016Review
- Modeling a Ca(2+) channel/BKCa channel complex at the single-complex level.Biophysical journal · 2014Article
- The smooth muscle-type β1 subunit potentiates activation by DiBAC4(3) in recombinant BK channels.Channels (Austin, Tex.) · 2014Article
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5 authors.
Funding
Abstract
Large conductance voltage and Ca(2+)-dependent K(+) channels (BK(Ca)) are activated by both membrane depolarization and intracellular Ca(2+). Recent studies on bacterial channels have proposed that a Ca(2+)-induced conformational change within specialized regulators of K(+) conductance (RCK) domains is responsible for channel gating. Each pore-forming alpha subunit of the homotetrameric BK(Ca) channel is expected to contain two intracellular RCK domains. The first RCK domain in BK(Ca) channels (RCK1) has been shown to contain residues critical for Ca(2+) sensitivity, possibly participating in the formation of a Ca(2+)-binding site. The location and structure of the second RCK domain in the BK(Ca) channel (RCK2) is still being examined, and the presence of a high-affinity Ca(2+)-binding site within this region is not yet established. Here, we present a structure-based alignment of the C terminus of BK(Ca) and prokaryotic RCK domains that reveal the location of a second RCK domain in human BK(Ca) channels (hSloRCK2). hSloRCK2 includes a high-affinity Ca(2+)-binding site (Ca bowl) and contains similar secondary structural elements as the bacterial RCK domains. Using CD spectroscopy, we provide evidence that hSloRCK2 undergoes a Ca(2+)-induced change in conformation, associated with an alpha-to-beta structural transition. We also show that the Ca bowl is an essential element for the Ca(2+)-induced rearrangement of hSloRCK2. We speculate that the molecular rearrangements of RCK2 likely underlie the Ca(2+)-dependent gating mechanism of BK(Ca) channels. A structural model of the heterodimeric complex of hSloRCK1 and hSloRCK2 domains is discussed.
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