Ion channels articles within Nature

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  • Article
    | Open Access

    A structure–function analysis of cystic fibrosis transmembrane conductance regulator shows its two nucleotide-binding domains dimerize before channel opening, and reveals a mechanism through which conformational changes in the channel regulate chloride conductance.

    • Jesper Levring
    • , Daniel S. Terry
    •  & Jue Chen
  • Article |

    Electrophysiological, structural and biochemical studies on the bestrophin-2 anion channel reveal asymmetric permeability to glutamate and show that it forms a cooperative machinery in complex with glutamine synthetase for glutamate release.

    • Aaron P. Owji
    • , Kuai Yu
    •  & Tingting Yang
  • Article |

    Cryo-electron microscopy reveals the structures of the mitochondrial calcium uniporter holocomplex in low- and high-calcium conditions, showing the gating mechanism that underlies uniporter activation in response to intracellular calcium signals.

    • Minrui Fan
    • , Jinru Zhang
    •  & Liang Feng
  • Article |

    The pore-forming and ATP-binding subunits of a mitochondrial protein complex that mediates ATP-dependent potassium currents are identified and characterized, revealing the role of this channel in mitochondrial physiology and pathologies.

    • Angela Paggio
    • , Vanessa Checchetto
    •  & Diego De Stefani
  • Article |

    Cryo-electron microscopy structures are reported in which the full-length human α1β3γ2L GABAA receptor in lipid nanodiscs is bound to the channel-blocker picrotoxin, the competitive antagonist bicuculline, the agonist GABA, and the benzodiazepines alprazolam and diazepam.

    • Simonas Masiulis
    • , Rooma Desai
    •  & A. Radu Aricescu
  • Article |

    Cryo-electron microscopy structures of connexin channels composed of connexin 46 and connexin 50 in an open-state reveal features that govern permselectivity and the location of mutated residues linked to herediatry cataracts.

    • Janette B. Myers
    • , Bassam G. Haddad
    •  & Steve L. Reichow
  • Article |

    The cryo-electron microscopy structure of the type A GABA receptor bound to GABA and the benzodiazepine site antagonist flumazenil reveals structural mechanisms that underlie intersubunit interactions and ligand selectivity of the receptor.

    • Shaotong Zhu
    • , Colleen M. Noviello
    •  & Ryan E. Hibbs
  • Article |

    The structure of a homomeric channel of subunit A of leucine-rich repeat-containing protein 8 (LRRC8) determined by cryo-electron microscopy and X-ray crystallography reveals the basis for anion selectivity.

    • Dawid Deneka
    • , Marta Sawicka
    •  & Raimund Dutzler
  • Article |

    The cryo-electron microscopy structure of full-length mouse Piezo1 reveals six Piezo repeats, and 26 transmembrane helices per protomer, and shows that a kinked helical beam and anchor domain link the Piezo repeats to the pore and control gating allosterically.

    • Kei Saotome
    • , Swetha E. Murthy
    •  & Andrew B. Ward
  • Letter |

    Single-particle electron cryo-microscopy analysis of the mechanotransduction channel NOMPC reveals that it contains a bundle of four helical spring-shaped ankyrin repeat domains that undergo motion, potentially allowing mechanical movement of the cytoskeleton to be coupled to the opening of the channel.

    • Peng Jin
    • , David Bulkley
    •  & Yifan Cheng
  • Letter |

    The crystal structure of the bacterial potassium import complex KdpFABC shows how ATP hydrolysis is coupled to potassium transport to maintain cellular homeostasis under low potassium conditions.

    • Ching-Shin Huang
    • , Bjørn Panyella Pedersen
    •  & David L. Stokes
  • Article |

    Two complementary studies present the full-length high-resolution structure of a Slo1 channel in the presence or absence of Ca2+ ions, in which an unconventional allosteric voltage-sensing mechanism regulates the Ca2+ sensor in addition to the voltage sensor’s direct action on the pore.

    • Xiao Tao
    • , Richard K. Hite
    •  & Roderick MacKinnon
  • Article |

    Two complementary studies present the full-length high-resolution structure of a Slo1 channel in the presence or absence of Ca2+ ions, in which an unconventional allosteric voltage-sensing mechanism regulates the Ca2+ sensor in addition to the voltage sensor’s direct action on the pore.

    • Richard K. Hite
    • , Xiao Tao
    •  & Roderick MacKinnon
  • Letter |

    Nicotinic acetylcholine receptors are ligand-gated ion channels that mediate fast chemical neurotransmission; here, the first X-ray crystal structure of a nicotinic receptor is reported, revealing how nicotine stabilizes the receptor in a non-conducting, desensitized conformation.

    • Claudio L. Morales-Perez
    • , Colleen M. Noviello
    •  & Ryan E. Hibbs
  • Article |

    The X-ray crystal structure of rat transient receptor potential channel TRPV6 at 3.25 Å resolution is reported, providing new insights into its assembly and calcium-selective permeation.

    • Kei Saotome
    • , Appu K. Singh
    •  & Alexander I. Sobolevsky
  • Article |

    Cryo-electron microscopy has undergone a resolution revolution—here, this method has been combined with lipid nanodisc technology to solve structures of TRPV1, the receptor for capsaicin, in a membrane bilayer, revealing mechanisms of lipid and ligand regulation.

    • Yuan Gao
    • , Erhu Cao
    •  & Yifan Cheng
  • Letter |

    The structure of the core region of the mitochondrial calcium uniporter (MCU) is determined by NMR and electron microscopy, revealing that MCU is a homo-pentamer with a specific transmembrane helix forming a hydrophilic pore across the membrane, and representing one of the largest membrane protein structures characterized by NMR spectroscopy.

    • Kirill Oxenoid
    • , Ying Dong
    •  & James J. Chou
  • Letter |

    Circadian rhythms in the intracellular concentration of magnesium ions act as a cell-autonomous timekeeping component to determine key clock properties and tune cellular metabolism both in a human cell line and in a unicellular alga.

    • Kevin A. Feeney
    • , Louise L. Hansen
    •  & Gerben van Ooijen
  • Article |

    This study has determined the electron cryomicroscopy structure of the mammalian type 1 InsP3 receptor in a ligand-free state at 4.7 Å resolution; although the central Ca2+-conduction pathway is similar to other ion channels, the unique architecture of the C-terminal domains of the tetrameric channel suggests that a distinctive allosteric mechanism underlies the activation of InsP3 gating.

    • Guizhen Fan
    • , Matthew L. Baker
    •  & Irina I. Serysheva
  • Article |

    Piezo1, a mechanosensitive cation channel, senses shear stress of blood flow for proper blood vessel development, regulates red blood cell function and controls cell migration and differentiation; here a trimeric architecture of this novel class of ion channel is reported, suggesting that Piezo1 may use its peripheral propeller-like ‘blades’ as force sensors to gate the central ion-conducting pore.

    • Jingpeng Ge
    • , Wanqiu Li
    •  & Maojun Yang
  • Article |

    A high-resolution electron cryo-microscopy structure of the zebrafish α1 glycine receptor bound to agonists or antagonists reveals the conformational changes that take place when the channel transitions from closed to open state.

    • Juan Du
    • , Wei Lü
    •  & Eric Gouaux
  • Letter |

    Microorganisms can export toxic fluoride ions through highly selective channels of the Fluc family; here, the crystal structures of two bacterial Fluc homologues are presented, revealing that selectivity for small F ions may arise from the proteins’ narrow pores and unusual anion coordination.

    • Randy B. Stockbridge
    • , Ludmila Kolmakova-Partensky
    •  & Simon Newstead
  • Article |

    The high-resolution electron cryo-microscopy structure of the full-length human TRPA1 ion channel is presented; the structure reveals a unique ankyrin repeat domain arrangement, a tetrameric coiled-coil in the centre of the channel that acts as a binding site for inositol hexakisphosphate, an outer poor domain with two pore helices, and a new drug binding site, findings that collectively provide mechanistic insight into TRPA1 regulation.

    • Candice E. Paulsen
    • , Jean-Paul Armache
    •  & David Julius
  • Article |

    Using electron cryomicroscopy, the structure of the closed-state rabbit ryanodine receptor RyR1 in complex with its modulator FKBP12 is solved at 3.8 Å; in addition to determining structural details of the ion-conducting channel domain, three previously uncharacterized domains help to reveal a molecular scaffold that allows long-range allosteric regulation of channel activities.

    • Zhen Yan
    • , Xiao-chen Bai
    •  & Nieng Yan
  • Letter |

    X-ray structures of the human TRAAK mechanosensitive potassium channel reveal how build-up of tension in the lipid membrane can convert the channel from a non-conducting wedge shape associated with an inserted lipid acyl chain that blocks the pore to an expanded cross-sectional shape that prevents lipid entry and thus permits ion conduction.

    • Stephen G. Brohawn
    • , Ernest B. Campbell
    •  & Roderick MacKinnon
  • Article |

    Using electron cryomicroscopy, the closed-state structure of rabbit RyR1 is determined at 4.8 Å resolution; analysis confirms that the RyR1 architecture consists of a six-transmembrane ion channel with a cytosolic α-solenoid scaffold, and suggests a mechanism for Ca2+-induced channel opening.

    • Ran Zalk
    • , Oliver B. Clarke
    •  & Andrew R. Marks