Sodium channels articles within Nature Communications

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  • Article
    | Open Access

    Cannabidiol (CBD), the nonpsychoactive component in cannabis, is an effective treatment for epilepsy and pain. Here, authors explored the mode of action of CBD on hNav1.7 channels through two distinct binding sites, suggesting a direct stabilization of the inactivated state of channels.

    • Jian Huang
    • , Xiao Fan
    •  & Nieng Yan

  • Article
    | Open Access

    Voltage-gated sodium (Nav) channels are targeted by various clinically applied and investigational drugs. Here cryo-EM structures of Nav1.7 bound to 7 compounds with diverse chemical skeletons reveal the structural basis of action of these drugs and provide a 3D structural map for drug binding sites on Nav channels.

    • Qiurong Wu
    • , Jian Huang
    •  & Nieng Yan

  • Article
    | Open Access

    Stings of certain ant species can cause intense, long-lasting nociception. Here, authors show that the major contributors of these symptoms are vertebrate-selective defensive venom peptides which modulate the activity of voltage-gated sodium channels.

    • Samuel D. Robinson
    • , Jennifer R. Deuis
    •  & Irina Vetter

  • Article
    | Open Access

    Voltage-gated sodium channels function as multiprotein signaling complexes. Here, authors show that the dispanin TMEM233 is essential for activity of stinging nettle toxins and that co-expression of TMEM233 modulates the gating properties of NaV1.7.

    • Sina Jami
    • , Jennifer R. Deuis
    •  & Irina Vetter

  • Article
    | Open Access

    Voltage-gated sodium channels mediate electrical signaling. Here, authors report the cryo-EM structure of NaVEh from the marine plant Emiliania huxleyi, revealing an unexpected mechanism of N-type fast inactivation.

    • Jiangtao Zhang
    • , Yiqiang Shi
    •  & Daohua Jiang

  • Article
    | Open Access

    Photoactivable toxins targeting ion channels have great potential to control cell activity. Here the authors report HwTxIV-Nvoc, a UV light-cleavable and photoactivatable peptide that targets voltage-gated sodium channels; they validate this in cells, brain slices and in vivo on mice neuromuscular junctions.

    • Jérôme Montnach
    • , Laila Ananda Blömer
    •  & Michel De Waard

  • Article
    | Open Access

    The role of of voltage-gated sodium channels (Nav) in pacemaking and conduction of the human sinoatrial node is unclear. Here, the authors investigate existence and function of neuronal and cardiac Nav in human sinoatrial nodes, and demonstrate their alterations in explanted human diseased hearts.

    • Ning Li
    • , Anuradha Kalyanasundaram
    •  & Vadim V. Fedorov

  • Article
    | Open Access

    Voltage-gated sodium (Nav) channels are crucial for action potential initiation in excitable cells. Here the authors present the complete structure of prokaryotic NavMs in a fully open state, providing structural insight into the opening and closure of the channel's intracellular gate.

    • Altin Sula
    • , Jennifer Booker
    •  & B. A. Wallace

  • Article
    | Open Access

    Restoring lost excitability of injured tissue is a paramount of regenerative medicine. By using a combined expression of bacterial voltage-gated Na+ channel, Kir2.1, and connexin-43 in non-excitable human fibroblasts, here the authors generate excitable cells that rescue action potential conduction in an in vitromodel of cardiac fibrosis.

    • Hung X. Nguyen
    • , Robert D. Kirkton
    •  & Nenad Bursac

  • Article
    | Open Access

    Cardiac voltage-gated sodium channels (Nav1.5) are crucial regulators of heart electric activity. Here the authors show that palmitoylation, a process of lipid modification of cysteine residues, modulates Nav1.5 function and affects cardiomyocyte excitability, representing a potential target in treating cardiac diseases.

    • Zifan Pei
    • , Yucheng Xiao
    •  & Theodore R. Cummins

  • Article
    | Open Access

    'Digital' spike-evoked transmission can be facilitated by slow subthreshold 'analogue' depolarisation of the presynaptic neuron. Here, the authors identify a novel, rapid form of digital-analogue facilitation in mammalian neurons whereby presynaptic hyperpolarisation enables de-inactivation of axonal Nav channels.

    • Sylvain Rama
    • , Mickaël Zbili
    •  & Dominique Debanne

  • Article
    | Open Access

    A mutation in the sodium channel Nav1.9 has been identified in a family and shown to associate with cold-aggravated pain. Here, the authors characterize the electrophysiological consequences of this mutation and propose a mechanism for the pain that the individuals experience.

    • Enrico Leipold
    • , Andrea Hanson-Kahn
    •  & Ingo Kurth

  • Article
    | Open Access

    Nav1.7 channels are known to regulate pain perception in humans and mice. Here, the authors provide evidence that Nav1.7 deletion leads to transcriptional upregulation of opioid peptides in sensory neurons, and that treatment with the opioid blocker naloxone helps reverse analgesia in mice and human Nav1.7 nulls.

    • Michael S. Minett
    • , Vanessa Pereira
    •  & John N. Wood

  • Article |

    Voltage-gated sodium channels (Nav) are transmembrane proteins that underlie action potentials in excitable tissues. Here, Gabelli et al. suggest a novel mechanism for the cytoplasmic control of switching from the inactivated to the non-inactivated form of the Nav1.5 channel that involves dimerization.

    • Sandra B. Gabelli
    • , Agedi Boto
    •  & L. Mario Amzel

  • Article
    | Open Access

    K+ channels are selective for K+ despite the fact that Na+ can bind and conduct through the selectivity filter. Sauer et al. show that a K+-selective NaK2K channel has two high-affinity K+-binding sites, whereas a non-selective NaK2CNG channel has one, and propose a double-barrier mechanism for ion selectivity.

    • David B. Sauer
    • , Weizhong Zeng
    •  & Youxing Jiang

  • Article
    | Open Access

    Prokaryotic voltage-gated sodium channels possess dynamically disordered cytoplasmic C-terminal domains. Bagnéris et al. present the structure of the Magnetococcus marinusNavMs pore and C-terminal domain and reveal its role in coupling channel inactivation and opening.

    • Claire Bagnéris
    • , Paul G. DeCaen
    •  & B. A. Wallace

  • Article
    | Open Access

    In outwardly rectifying potassium channels, depolarization initiates conformational changes in voltage-sensing domains. Goldschen-Ohmet al. find that movement of three specific domains correlates with conductance levels, and rearrangements of a fourth domain results in preinactivation subconductance states.

    • Marcel P. Goldschen-Ohm
    • , Deborah L. Capes
    •  & Baron Chanda

  • Article
    | Open Access

    Sodium-gated ion channels open and close in response to the flow of ions. Here, McCusker et al.report the open structure of a sodium-gated ion channel pore from a bacterial homologue, and show, by comparison with the closed structure, that the movement of a C-terminal helix is sufficient to open the channel.

    • Emily C. McCusker
    • , Claire Bagnéris
    •  & B.A. Wallace

  • Article |

    Perturbation of the cardiac voltage-gated sodium channel, NaV1.5, by drugs or inherited mutation can underlie and trigger cardiac arrhythmias. Here, the role of the NaV1.5 carboxy terminus in channel inactivation is investigated, and structural details of an arrhythmia associated H6 mutant are reported.

    • Ian W. Glaaser
    • , Jeremiah D. Osteen
    •  & Robert S. Kass

  • Article |

    Class I anti-arrhythmic drugs act at cardiac sodium channels and are subdivided into classes Ia-c based on their effects on the electrocardiogram. Here, class Ib drugs are found to rely on cation–pi interactions for their activity, whereas class Ib and Ic drugs rely significantly less on this interaction.

    • Stephan A. Pless
    • , Jason D. Galpin
    •  & Christopher A. Ahern

  • Article
    | Open Access

    In vitrostudies have suggested that the ubiquitin ligase, Nedd4-2, regulates several proteins, including the epithelial sodium channel. Here by examining Nedd4-2-deficient mice, the authors demonstrate that Nedd4-2 is essential for epithelial sodium channel regulation, fetal and postnatal lung function and animal survival.

    • Natasha A. Boase
    • , Grigori Y. Rychkov
    •  & Sharad Kumar

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