ArticleBiophysical journal2006
Tuning magnesium sensitivity of BK channels by mutations.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Magnesium Ions as Modulators of Voltage-Gated and Ligand-Gated Ion Channels in Central Neurons.International journal of molecular sciences · 2025Review
- 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
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- Interactions of divalent cations with calcium binding sites of BK channels reveal independent motions within the gating ring.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- BK channels: multiple sensors, one activation gate.Frontiers in physiology · 2015Review
- Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Ca2+ block and flickering both contribute to the negative slope of the IV curve in BK channels.The Journal of general physiology · 2013Article
- Mg(2+) binding to open and closed states can activate BK channels provided that the voltage sensors are elevated.The Journal of general physiology · 2011Article
- 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
- Mg2+-dependent regulation of BK channels: importance of electrostatics.The Journal of general physiology · 2008Article
- Mg2+ mediates interaction between the voltage sensor and cytosolic domain to activate BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Intracellular Mg(2+) at physiological concentrations activates mSlo1 BK channels by binding to a metal-binding site in the cytosolic domain. Previous studies suggest that residues E374, Q397, and E399 are important in Mg(2+) binding. In the present study, we show that mutations of E374 or E399 to other amino acids, except for Asp, abolish Mg(2+) sensitivity. These results further support that the side chains of E374 and E399 are essential for Mg(2+) coordination. To the contrary, none of the Q397 mutations abolishes Mg(2+) sensitivity, suggesting that its side chain may not coordinate to Mg(2+). However, because Q397 is spatially close to E374 and E399, its mutations affect the Mg(2+) sensitivity of channel gating by either reducing or increasing the Mg(2+) binding affinity. The pattern of mutational effects and the effect of chemical modification of Q397C indicate that Q397 is involved in the Mg(2+)-dependent activation of BK channels and that mutations of Q397 alter Mg(2+) sensitivity by affecting the conformation of the Mg(2+) binding site as well as by electrostatic interactions with the bound Mg(2+) ion.
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Registered trials
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