Potassium channels articles within Nature Communications

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  • Article
    | Open Access

    Using computer simulations authors identify the dynamic molecular motions controlling the structural conformation of the TWIK1 ion channel, showing that its ability to transport sodium upon acidification result from the evolution of the classical potassium-selective pore.

    • Franck C. Chatelain
    • , Nicolas Gilbert
    •  & Olivier Bignucolo

  • Article
    | Open Access

    Progesterone is used in recovery of cerebral ischemia however the mechanism of action is unknown. Authors report here that micromolar progesterone activates mouse cerebrovascular myocyte BK channels, involving two steroid binding sites.

    • Kelsey C. North
    • , Andrew A. Shaw
    •  & Alex M. Dopico

  • Article
    | Open Access

    The potassium channel KCNQ2 can be activated by analgesics and antiepileptic drugs via an unclear mechanism. Here authors report structures of KCNQ2-CaM in complex with cannabidiol, PIP2, and HN37 and elucidate the mechanisms of activation.

    • Demin Ma
    • , Yueming Zheng
    •  & Jiangtao Guo

  • Article
    | Open Access

    Potassium channels allow vital organ such as brain, heart, and muscles to function. Here, authors reveal the existence of a noncanonical kinematic chain of residues involving the S4/S1 and S1/S5 subunit interfaces that controls the gating of the hERG cardiac channel.

    • Carlos A. Z. Bassetto Jr
    • , Flavio Costa
    •  & Alberto Giacomello

  • Article
    | Open Access

    The potassium channel selectivity filter is responsible for conduction and selectivity of K + over other cations. Here, the authors use a combination of single molecule FRET, non-canonical fluorescent amino acid incorporation, and single channel patch-clamp electrophysiology, to establish the generality of K + -induced SF conformational stability across the K + channel superfamily.

    • Marcos Matamoros
    • , Xue Wen Ng
    •  & Colin G. Nichols

  • Article
    | Open Access

    Arabidopsis thaliana potassium channel AKT1 is responsible for primary K + uptake from soil, which is functionally activated through phosphorylation and negatively regulated by an α-subunit AtKC1. Here, the authors report the structures of AKT1 at different states, revealing a 2- fold to 4-fold symmetry switch at cytoplasmic domain associated with AKT1 activity regulation.

    • Yaming Lu
    • , Miao Yu
    •  & Guanghui Yang

  • Article
    | Open Access

    Here, Chi et al. report cryo-EM structures of the human Kv3.1a channel, revealing a unique arrangement of the cytoplasmic T1 domain, which allows the interactions with the C-terminal axonal targeting motif and key components of the gating machinery. These findings provide insights into the functional relevance of previously unknown interdomain interactions in Kv3 channels and may guide the design of new pharmaceutical drugs.

    • Gamma Chi
    • , Qiansheng Liang
    •  & Katharina L. Dürr

  • Article
    | Open Access

    The Kv1.3 potassium channel is expressed abundantly on activated T cells and mediates the cellular immune responses. Here, the authors report structures of the Kv1.3 potassium channel with and without immunoglobulin modulators, shedding light on the mechanisms of Kv1.3 gating and modulation.

    • Purushotham Selvakumar
    • , Ana I. Fernández-Mariño
    •  & Joel R. Meyerson

  • Article
    | Open Access

    TWIK1 is a pH-gated K + channel highly expressed in brain and heart that contributes to cardiac rhythm and insulin release. Here, Turney et al. use cryo-EM and electrophysiology to show how TWIK1 gates closed in response to lowered pH through conformational changes centered at the selectivity filter.

    • Toby S. Turney
    • , Vivian Li
    •  & Stephen G. Brohawn

  • Article
    | Open Access

    SUR2-containing KATP channels are drug targets for certain vasodilators. Here, the authors determine high-resolution cryo-EM structures of SUR2 in complex with two vasodilators, P1075 and levcromakalim, uncovering the mechanisms of these drugs.

    • Dian Ding
    • , Jing-Xiang Wu
    •  & Lei Chen

  • Article
    | Open Access

    Physiological matching of blood flow to the demand for oxygen by the heart is required for sustained cardiac health, yet the underlying mechanisms are obscure. Here, the authors report a key role for acute modifications to the redox state of intracellular pyridine nucleotides in coronary smooth muscle and their impact on voltage-gated K + channels in metabolic vasodilation

    • Marc M. Dwenger
    • , Sean M. Raph
    •  & Matthew A. Nystoriak

  • Article
    | Open Access

    Constriction of the selectivity filter is assumed to be a hallmark of C-type inactivation in K+ channels. Using different high-resolution methods, this study shows a distinct C-type inactivation mechanism in a KcsA mutant that emulates Kv-channels.

    • Ahmed Rohaim
    • , Bram J. A. Vermeulen
    •  & Markus Weingarth

  • Article
    | Open Access

    The Kir potassium channels are known to operate and gate without a major conformational change. Here, the authors identify the permeation gate of Kir channels as a steric plug within the conduction pathway, describing how tightly associated anionic lipids pushing into fenestrations in the pore walls engage with the plug to operate the gate.

    • Ruitao Jin
    • , Sitong He
    •  & Jacqueline M. Gulbis

  • Article
    | Open Access

    Slowpoke (Slo) channels are voltage-gated potassium channels that are activated by high intracellular Ca2+ concentrations, and they are targets for insecticides and antiparasitic drugs. Here, the authors present the cryo-EM structures of the Drosophila melanogaster Slo channel in the Ca2+-bound and Ca2+-free conformations, as well as in complex with the fungal neurotoxin verruculogen and the anthelmintic drug emodepside and discuss the mechanisms by which they affect the activity of Slo.

    • Tobias Raisch
    • , Andreas Brockmann
    •  & Stefan Raunser

  • Article
    | Open Access

    Here, the authors perform a large-scale, high-throughput biochemical assay to determine the compatibility of over 300,000 domain recombination variants of the inward rectifier K+ channel Kir2.1. They derive rules for designing domain insertion variants that fold and traffic to the cell surface and conclude that the insertion of domains at protein termini is evolutionary favoured.

    • Willow Coyote-Maestas
    • , David Nedrud
    •  & Daniel Schmidt

  • Article
    | Open Access

    NaK is a bacterial non-selective cation channel. Here, the authors use solution NMR to show that selectivity filter (SF) in NaK is dynamic, with structural differences between the Na+ and K + -bound states. The conformation of the SF is communicated to the pore-lining helices similarly as in the K + -selective channels.

    • Adam Lewis
    • , Vilius Kurauskas
    •  & Katherine Henzler-Wildman

  • Article
    | Open Access

    KdpFABC is a high-affinity bacterial K+ pump which combines the ion channel-like KdpA and the P-type ATPase KdpB. Here, the authors elucidate the mechanisms underlying transport and the coupling to ATP hydrolysis, and provide evidence that ions are transported via an intersubunit tunnel through KdpA and KdpB.

    • Jakob M. Silberberg
    • , Robin A. Corey
    •  & Inga Hänelt

  • Article
    | Open Access

    Potassium ion channels control K+ permeation across cell membranes and mutations that cause cardiovascular and neural diseases are known. Here, the authors perform NMR measurements with the prototypical K+ channel from Streptomyces lividans, KcsA and characterise the effects of disease causing mutations on the conformational dynamics of K+ channels in a physiological solution environment.

    • Yuta Iwahashi
    • , Yuki Toyama
    •  & Ichio Shimada

  • Article
    | Open Access

    Opening of G protein-gated inwardly rectifying potassium channels (GIRK) is coupled to the activation of a GPCR. Here the authors use NMR and cell-based BRET assays to gain insights into the mechanisms underlying family-specific activation and find that pre-formation of the Gαi/oβγ-GIRK complex in the inactive state is responsible for specific GIRK activation and present a structural model for the Gαi/oβγ-GIRK complex.

    • Hanaho Kano
    • , Yuki Toyama
    •  & Ichio Shimada

  • Article
    | Open Access

    Allostery is a fundamental principle of protein regulation that remains challenging to engineer. Here authors screen human Inward Rectifier K + Channel Kir2.1 for permissibility to domain insertions and propose that differential permissibility is a metric of latent allosteric capacity in Kir2.1.

    • Willow Coyote-Maestas
    • , Yungui He
    •  & Daniel Schmidt

  • Article
    | Open Access

    Spontaneous activity shifts at constant experimental conditions are widespread among ion channels but the molecular origins are poorly understood. Here, using solid-state NMR and MD simulations, the authors reveal that modal gating shifts in K + channels are caused by large shifts in the channel dynamics which perturb the selectivity filter.

    • Shehrazade Jekhmane
    • , João Medeiros-Silva
    •  & Markus Weingarth

  • Article
    | Open Access

    The number of K+ occupied binding sites in the selectivity filter of potassium ion channels is still under debate. Here, the authors collect diffraction data on the K+ selective NaK channel NaK2K at a wavelength of 3.35 Å, close to the K absorption edge, revealing that all four binding sites in the selectivity filter are fully occupied by K+ ions.

    • Patricia S. Langan
    • , Venu Gopal Vandavasi
    •  & Leighton Coates

  • Article
    | Open Access

    Despite being highly toxic, carbon monoxide (CO) is also essential as an intracellular signalling molecule, but CO-dependent signalling is poorly understood. Here, authors employ spectroscopic and electrophysiology methods and find that CO activates KATP channels via SUR2A, a heme-regulated receptor.

    • Sofia M. Kapetanaki
    • , Mark J. Burton
    •  & Emma Raven

  • Article
    | Open Access

    TREKs are members of the two-pore domain potassium (K2P) channels, being important clinical targets. Here the authors identify inhibitors of K2P that bind to an allosteric site located in their extracellular cap, suggesting that it might be a promising drug target for these channels.

    • Qichao Luo
    • , Liping Chen
    •  & Huaiyu Yang

  • Article
    | Open Access

    Trimeric intracellular cation channels (TRICs) elicit K+ currents to counteract luminal negative potential during Ca2+release from intracellular stores. Here the authors present structures of prokaryotic TRICs in their open and closed states, obtaining molecular insight into TRICs’ function.

    • Min Su
    • , Feng Gao
    •  & Yu-hang Chen

  • Article
    | Open Access

    Episodic ataxia type 1 is caused by mutations in the potassium channel Kv1.1, which is found in cerebellar basket cells. Here, the authors use electrophysiology techniques to characterize these mutant channels, and observe that the changes result in decreased spontaneous Purkinje cell firing with no evidence for developmental compensation.

    • Rahima Begum
    • , Yamina Bakiri
    •  & Dimitri M. Kullmann

  • Article
    | Open Access

    Long-term use of opioids can lead to a paradoxical increase in pain sensitivity. Here, Hayashi et al. link activation of potassium channels on microglia with morphine-induced hyperalgesia and anti-nociceptive tolerance in mice.

    • Yoshinori Hayashi
    • , Saori Morinaga
    •  & Hiroshi Nakanishi

  • Article
    | Open Access

    Potassium channels in the ventral tegmental area are known to regulate resilience against stress-induced depression. Here, the authors show over expression of KCNQ3 channels in VTA dopaminergic neurons or treatment with KCNQ channel openers normalizes depressive behaviours in mouse models.

    • Allyson K. Friedman
    • , Barbara Juarez
    •  & Ming-Hu Han

  • Article
    | Open Access

    The neural mechanisms underlying efficient coding of natural sensory stimuli have yet to be fully determined. Here, monitoring sensory pyramidal cells in weakly electric fish, the authors find SK channels are necessary for matching the responsiveness of neurons to natural stimuli and subsequent behavioural responses.

    • Chengjie G. Huang
    • , Zhubo D. Zhang
    •  & Maurice J. Chacron

  • Article
    | Open Access

    BK potassium channels have been previously shown to mediate SCN circadian firing, although the precise mechanisms are unclear. Here, using knockout and rescue approaches, the authors find that the ß2 ‘ball-and-chain’ confers BK channel inactivation during the day, promoting SCN electrical upstate.

    • Joshua P. Whitt
    • , Jenna R. Montgomery
    •  & Andrea L. Meredith

  • Article
    | Open Access

    Kv3 potassium channels have an important role in the repolarization of action potentials in fast-spiking neurons. Here, the authors use electrophysiology and modelling to report on an interesting mechanism that might explain their gating behaviour.

    • Alain J. Labro
    • , Michael F. Priest
    •  & Francisco Bezanilla

  • Article
    | Open Access

    Potassium is necessary for the mechanical-electrical transduction needed for hearing. Here the authors study mice lacking the potassium channel KCNK5 and show that these channels are mostly expressed in the outer sulcus and are required for hearing, pointing to their essential role in potassium recycling.

    • Yves Cazals
    • , Michelle Bévengut
    •  & Christian Gestreau

  • Article
    | Open Access

    Ion channels open and close to allow the regulated passage of ions through the membrane. Here the authors use selective ion channel blockers to analyse this regulation in a potassium channel and show that the gate is in the selectivity filter, past the entrance to the channel.

    • David J. Posson
    • , Radda Rusinova
    •  & Crina M. Nimigean

  • Article
    | Open Access

    Ion channels are often an assembly of proteins, but it is not clear if protein combinations have additive effects or function to prevent binding of other proteins. Here, the authors show that β and γ subunits can assemble into the same BK complex, and the constituents of the complex have an effect on its function.

    • Vivian Gonzalez-Perez
    • , Xiao-Ming Xia
    •  & Christopher J. Lingle

  • Article
    | Open Access

    The pore of voltage-gated ion channels opens in response to membrane depolarization sensed by a separate voltage-sensing domain. Here, Lörinczi et al. show that, contrary to assumptions, no physical linker is required to transmit changes from the voltage-sensing to the permeation domain of KCNH channels.

    • Éva Lörinczi
    • , Juan Camilo Gómez-Posada
    •  & Luis A. Pardo

  • Article |

    Type 2 Long QT syndrome is a cardiac disease associated with hundreds of individual mutations within the Kv11.1 potassium channel. Here, the authors systematically investigate the trafficking defects associated with different types of Kv11.1 mutations and to what extent they can be corrected pharmacologically.

    • Corey L. Anderson
    • , Catherine E. Kuzmicki
    •  & Craig T. January

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