Ion transport articles within Nature

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  • Article
    | Open Access

    Screening in Escherichia coli and biochemical experiments show that in Arabidopsis thaliana, OSCA2.1 and OSCA2.2 function as plant sensors of hypo-osmolarity, utilize Ca2+ oscillations as second messengers and have crucial roles in pollen germination.

    • Songyu Pei
    • , Qi Tao
    •  & Fang Yuan

  • Article |

    High-speed atomic force microscopy single-molecule imaging and cryo-EM analysis discover and reveal the structure of a TRPV3 pentamer, providing evidence for a non-canonical pentameric TRP-channel assembly, laying the foundation for new directions in TRP channel research.

    • Shifra Lansky
    • , John Michael Betancourt
    •  & Simon Scheuring

  • 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 structures of the bacterial protein machinery that is involved in the production and function of nitrous oxide provide insight into the assembly pathway of this enzyme and the mechanisms of copper transport.

    • Christoph Müller
    • , Lin Zhang
    •  & Oliver Einsle

  • Article |

    Cryo-electron microscopy structures of GABAA receptors bound to intravenous anaesthetics and benzodiazepines reveal both common and distinct transmembrane binding sites, and show that the mechanisms of action of anaesthetics partially overlap with those of benzodiazepines.

    • Jeong Joo Kim
    • , Anant Gharpure
    •  & Ryan E. Hibbs

  • Article |

    Cryo-electron microscopy structures and molecular dynamics simulations of the calcium-activated potassium channel MthK from Methanobacterium thermoautotrophicum are used to show that gating of this channel involves a ball-and-chain inactivation mechanism mediated by a previously unresolved N-terminal peptide.

    • Chen Fan
    • , Nattakan Sukomon
    •  & Crina M. Nimigean

  • Article |

    An in vivo approach to identify proteins whose enrichment near cardiac CaV1.2 channels changes upon β-adrenergic stimulation finds the G protein Rad, which is phosphorylated by protein kinase A, thereby relieving channel inhibition by Rad and causing an increased Ca2+ current.

    • Guoxia Liu
    • , Arianne Papa
    •  & Steven O. Marx

  • Article |

    Imaging of substrate transport by individual MhsT transporters, members of the neurotransmitter:sodium symporter family of secondary transporters, at single- and multi-turnover resolution reveals that the rate-limiting step varies with the identity of the transported substrate.

    • Gabriel A. Fitzgerald
    • , Daniel S. Terry
    •  & Scott C. Blanchard

  • Article |

    Cryo-electron microscopy and high-speed atomic force microscopy reveal that PIEZO1 can reversibly deform its shape towards a planar structure, which may explain how the PIEZO1 channel is gated in response to mechanical stimulation.

    • Yi-Chih Lin
    • , Yusong R. Guo
    •  & Simon Scheuring

  • 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 |

    Crystal structures and molecular simulations of the designed anion-conducting channelrhodopsin iC++ provide molecular insights that enable structure-based design of channelrhodopsins with desirable properties for use as optogenetic tools.

    • Hideaki E. Kato
    • , Yoon Seok Kim
    •  & Karl Deisseroth

  • 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 |

    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

  • Brief Communications Arising |

    • Mei-ling A. Joiner
    • , Olha M. Koval
    •  & Mark E. Anderson

  • Article |

    An X-ray structure and electrophysiological analysis of mammalian G-protein-gated inward rectifier potassium channel GIRK2 in complex with βγ reveals a pre-open channel structure consistent with channel activation by membrane delimited G-protein subunits.

    • Matthew R. Whorton
    •  & Roderick MacKinnon

  • Letter |

    The X-ray crystal structure of a member of the Ca2+/H+ (CAX) antiporter family from Saccharomyces cerevisiae in a cytosol-facing, substrate-bound conformation is solved; using the structure, a mechanism by which members of the Ca2+:cation (CaCA) superfamily facilitate Ca2+ transport across cellular membranes is proposed.

    • Andrew B. Waight
    • , Bjørn Panyella Pedersen
    •  & Robert M. Stroud

  • Letter |

    The X-ray crystal structure of a high-affinity phosphate importer in an inward-facing, occluded state in the presence of phosphate is reported; this is the first structure of a membrane protein involved in inorganic phosphate uptake and the first crystal structure of a eukaryotic MFS transporter.

    • Bjørn P. Pedersen
    • , Hemant Kumar
    •  & Robert M. Stroud

  • Letter |

    The cytosolic concentration of citrate partially depends on its direct import across the plasma membrane by the Na+-dependent citrate transporter (NaCT); here the X-ray crystal structure of a bacterial homologue of NaCT is reported, which, along with transport-activity studies, suggests how specific conformational changes facilitate substrate translocation across the cellular membrane.

    • Romina Mancusso
    • , G. Glenn Gregorio
    •  & Da-Neng Wang

  • Letter |

    Transport of solutes across biological membranes is carried out by specialized secondary transport proteins in the lipid bilayer. These authors report structures of the sodium-independent carnitine/butyrobetaine antiporter CaiT from two microorganisms. The three-dimensional architecture of CaiT resembles that of the Na+-dependent transporters LeuT and BetP, but in CaiT a methionine sulphur takes the place of the Na+ ion to coordinate the substrate in the central transport site, enabling Na+-independent transport to occur.

    • Sabrina Schulze
    • , Stefan Köster
    •  & Werner Kühlbrandt

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