ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013
The interface between membrane-spanning and cytosolic domains in Ca²+-dependent K+ channels is involved in β subunit modulation of gating.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Distinct domains of the β1-subunit cytosolic N terminus control surface expression and functional properties of large-conductance calcium-activated potassium (BK) channels.The Journal of biological chemistry · 2017Article
- Deletion of cytosolic gating ring decreases gate and voltage sensor coupling in BK channels.The Journal of general physiology · 2017Article
- The unique N-terminal sequence of the BKCa channel α-subunit determines its modulation by β-subunits.PloS one · 2017Article
- Alcohol modulation of BK channel gating depends on β subunit composition.The Journal of general physiology · 2016Article
- Modulation of BK Channel Function by Auxiliary Beta and Gamma Subunits.International review of neurobiology · 2016Review
- Two classes of regulatory subunits coassemble in the same BK channel and independently regulate gating.Nature communications · 2015Article
- Molecular mechanism underlying β1 regulation in voltage- and calcium-activated potassium (BK) channels.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural basis for calcium and magnesium regulation of a large conductance calcium-activated potassium channel with β1 subunits.The Journal of biological chemistry · 2014Article
- N-terminal isoforms of the large-conductance Ca²⁺-activated K⁺ channel are differentially modulated by the auxiliary β1-subunit.The Journal of biological chemistry · 2014Article
- A microscopic view of phospholipid insertion into biological membranes.The journal of physical chemistry. B · 2014Article
- Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Large-conductance, voltage-, and Ca²⁺-dependent K⁺ (BK) channels are broadly expressed in various tissues to modulate neuronal activity, smooth muscle contraction, and secretion. BK channel activation depends on the interactions among the voltage sensing domain (VSD), the cytosolic domain (CTD), and the pore gate domain (PGD) of the Slo1 α-subunit, and is further regulated by accessory β subunits (β1-β4). How β subunits fine-tune BK channel activation is critical to understand the tissue-specific functions of BK channels. Multiple sites in both Slo1 and the β subunits have been identified to contribute to the interaction between Slo1 and the β subunits. However, it is unclear whether and how the interdomain interactions among the VSD, CTD, and PGD are altered by the β subunits to affect channel activation. Here we show that human β1 and β2 subunits alter interactions between bound Mg²⁺ and gating charge R213 and disrupt the disulfide bond formation at the VSD-CTD interface of mouse Slo1, indicating that the β subunits alter the VSD-CTD interface. Reciprocally, mutations in the Slo1 that alter the VSD-CTD interaction can specifically change the effects of the β1 subunit on the Ca²⁺ activation and of the β2 subunit on the voltage activation. Together, our data suggest a novel mechanism by which the β subunits modulated BK channel activation such that a β subunit may interact with the VSD or the CTD and alter the VSD-CTD interface of the Slo1, which enables the β subunit to have effects broadly on both voltage and Ca²⁺-dependent activation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.