ArticleBiophysical journal2008
Modulation of the conductance-voltage relationship of the BK Ca channel by mutations at the putative flexible interface between two RCK domains.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Incorporating physics to overcome data scarcity in predictive modeling of protein function: A case study of BK channels.PLoS computational biology · 2023Article
- Incorporating physics to overcome data scarcity in predictive modeling of protein function: a case study of BK channels.bioRxiv : the preprint server for biology · 2023Article
- Effects of Single Nucleotide Polymorphisms in HumanFrontiers in molecular neuroscience · 2019Article
- Combining fragment homology modeling with molecular dynamics aims at prediction of Ca²⁺ binding sites in CaBPs.Journal of computer-aided molecular design · 2013Article
- On the simple random-walk models of ion-channel gate dynamics reflecting long-term memory.European biophysics journal : EBJ · 2012Article
- TRPC6 channels and their binding partners in podocytes: role in glomerular filtration and pathophysiology.American journal of physiology. Renal physiology · 2010Review
- BK channel activation: structural and functional insights.Trends in neurosciences · 2010Review
- The RCK1 domain of the human BKCa channel transduces Ca2+ binding into structural rearrangements.The Journal of general physiology · 2010Article
- Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution.Science (New York, N.Y.) · 2010Article
- Modulation of the conductance-voltage relationship of the BK(Ca) channel by shortening the cytosolic loop connecting two RCK domains.Biophysical journal · 2009Article
- Measurements of the BKCa channel's high-affinity Ca2+ binding constants: effects of membrane voltage.The Journal of general physiology · 2008Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Calcium-dependent gating of the large-conductance Ca(2+)-activated K(+) (BK(Ca)) channel is conferred by the large cytosolic carboxyl terminus containing two domains of the regulator of K(+) conductance (RCK) and the high-affinity Ca(2+)-binding site (the Ca(2+)-bowl). In our previous study, we located the putative second RCK domain (RCK2) and demonstrated that it interacts directly with RCK1 via a hydrophobic "assembly interface". In this study, we tested the structural model of the other interface, the "flexible interface", by strategically positioning charge pairs across the putative interface. Several charge mutations on RCK2 affected the voltage-dependent activation of the channel. In particular, the Gly-to-Asp substitution at position 803 profoundly affected channel activation by stabilizing the open conformation of the channel with minimal effects on its Ca(2+) affinity and voltage sensitivity. Various mutations at Gly-803 shifted the channel's conductance-voltage curve either left or right over a 145-mV range. Since this residue is predicted to be in the first loop of RCK2 these results strongly suggest that this loop plays a critical role in determining the intrinsic equilibrium constant for channel opening, and they support the hypothesis that this loop is part of an interface that mediates conformational coupling between RCK1 and RCK2.
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