ArticleThe Journal of general physiology2005
Cysteine modification alters voltage- and Ca(2+)-dependent gating of large conductance (BK) potassium channels.
Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Redox Regulation of KAntioxidants & redox signaling · 2024Review
- Carotid body chemoreceptors: physiology, pathology, and implications for health and disease.Physiological reviews · 2021Review
- Effects of Single Nucleotide Polymorphisms in HumanFrontiers in molecular neuroscience · 2019Article
- Dihydromyricetin improves vascular hyporesponsiveness in experimental sepsis via attenuating the over-excited MaxiK and KPharmaceutical biology · 2018Article
- Identification of Cav2-PKCβ and Cav2-NOS1 complexes as entities for ultrafast electrochemical coupling.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Closed state-coupled C-type inactivation in BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Ziram, a pesticide associated with increased risk for Parkinson's disease, differentially affects the presynaptic function of aminergic and glutamatergic nerve terminals at the Drosophila neuromuscular junction.Experimental neurology · 2016Article
- Oxidative Stress and Maxi Calcium-Activated Potassium (BK) Channels.Biomolecules · 2015Review
- Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Redox and nitric oxide-mediated regulation of sensory neuron ion channel function.Antioxidants & redox signaling · 2015Review
- Paxilline inhibits BK channels by an almost exclusively closed-channel block mechanism.The Journal of general physiology · 2014Article
- Oxidative modulation of voltage-gated potassium channels.Antioxidants & redox signaling · 2014Review
- The interface between membrane-spanning and cytosolic domains in Ca²+-dependent K+ channels is involved in β subunit modulation of gating.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Interaction between residues in the Mg2+-binding site regulates BK channel activation.The Journal of general physiology · 2013Article
- Charge substitution for a deep-pore residue reveals structural dynamics during BK channel gating.The Journal of general physiology · 2011Article
- Cysteine scanning and modification reveal major differences between BK channels and Kv channels in the inner pore region.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Inhibition of large-conductance Ca2+-activated K+ channels by nanomolar concentrations of Ag+.Molecular pharmacology · 2010Article
- Differential effect of L-cysteine in isolated whole-bladder preparations from neonatal and adult rats.The Journal of pharmacology and experimental therapeutics · 2010Article
- Activation of Slo1 BK channels by Mg2+ coordinated between the voltage sensor and RCK1 domains.Nature structural & molecular biology · 2008Article
- Mg2+ enhances voltage sensor/gate coupling in BK channels.The Journal of general physiology · 2008Article
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2 authors.
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Abstract
The Ca(2+)-activated K+ (BK) channel alpha-subunit contains many cysteine residues within its large COOH-terminal tail domain. To probe the function of this domain, we examined effects of cysteine-modifying reagents on channel gating. Application of MTSET, MTSES, or NEM to mSlo1 or hSlo1 channels changed the voltage and Ca2+ dependence of steady-state activation. These reagents appear to modify the same cysteines but have different effects on function. MTSET increases I(K) and shifts the G(K)-V relation to more negative voltages, whereas MTSES and NEM shift the G(K)-V in the opposite direction. Steady-state activation was altered in the presence or absence of Ca2+ and at negative potentials where voltage sensors are not activated. Combinations of [Ca2+] and voltage were also identified where P(o) is not changed by cysteine modification. Interpretation of our results in terms of an allosteric model indicate that cysteine modification alters Ca2+ binding and the relative stability of closed and open conformations as well as the coupling of voltage sensor activation and Ca2+ binding and to channel opening. To identify modification-sensitive residues, we examined effects of MTS reagents on mutant channels lacking one or more cysteines. Surprisingly, the effects of MTSES on both voltage- and Ca(2+)-dependent gating were abolished by replacing a single cysteine (C430) with alanine. C430 lies in the RCK1 (regulator of K+ conductance) domain within a series of eight residues that is unique to BK channels. Deletion of these residues shifted the G(K)-V relation by > -80 mV. Thus we have identified a region that appears to strongly influence RCK domain function, but is absent from RCK domains of known structure. C430A did not eliminate effects of MTSET on apparent Ca2+ affinity. However an additional mutation, C615S, in the Haem binding site reduced the effects of MTSET, consistent with a role for this region in Ca2+ binding.
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