Ion channels articles within Nature

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  • Article |

    Using electron cryomicroscopy, the structure of the rabbit RyR1 calcium channel is determined at 6.1 Å resolution in the closed state and 8.5 Å in the open state, revealing how calcium binding to the EF-hand of RyR1 regulates channel opening and facilitates calcium-induced calcium release.

    • Rouslan G. Efremov
    • , Alexander Leitner
    •  & Stefan Raunser

  • Article |

    The authors describe the structure of a Ca2+-activated lipid scramblase which catalyses the passive movement of lipids between the two leaflets of a lipid bilayer; the structure reveals the location of a regulatory calcium-binding site embedded within the membrane and the presence of a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer, where catalysis is likely to occur.

    • Janine D. Brunner
    • , Novandy K. Lim
    •  & Raimund Dutzler

  • Article |

    The X-ray crystal structure of a eukaryotic Ca2+-activated chloride channel, BEST1, and its function in liposomes are described; the structure shows that Ca2+ binds to the cytosolic region of this pentameric channel and reveals that the pore is approximately 95 Å long with at least 15 distinct anion-binding sites.

    • Veronica Kane Dickson
    • , Leanne Pedi
    •  & Stephen B. Long

  • Letter |

    This study solved structures of the glutamate-gated chloride channel (GluCl), a Cys-loop receptor from C. elegans, in an apo, closed state and in a lipid-bound state — comparison of these structures with a previously published structure of GluCl in an ivermectin-bound state reveals what conformational changes probably occur as this membrane protein transitions from the closed/resting state towards an open/activated state.

    • Thorsten Althoff
    • , Ryan E. Hibbs
    •  & Eric Gouaux

  • Article |

    The first X-ray crystal structure of the mouse serotonin 5-HT3 receptor, a pentameric ligand-gated ion channel, is similar to those of other Cys-loop receptors — though here electron density for part of the cytoplasmic domain, which is important for trafficking, synaptic localization, and modulation by cytoplasmic proteins, but not visible in previous structures, is also described.

    • Ghérici Hassaine
    • , Cédric Deluz
    •  & Hugues Nury

  • Outlook |

    Epilepsy is one of the most common neurological disorders to affect the human brain. Many genetic aspects of the disease have been identified, but mechanisms remains elusive.

    • Charvy Narain

  • Article |

    GABAA receptors are the principal mediators of rapid inhibitor synaptic transmission in the brain, and a decline in GABAA signalling leads to diseases including epilepsy, insomnia, anxiety and autism; here, the first X-ray crystal structure of a human GABAA receptor, the human β3 homopentamer, reveals structural features unique for this receptor class and uncovers the locations of key disease-causing mutations.

    • Paul S. Miller
    •  & A. Radu Aricescu

  • Article |

    Using a peptide toxin and small vanilloid agonists as pharmacological probes, high-resolution electron cryo-microscopy structures of rat TRPV1–ligand complexes are solved; these structures highlight conformational differences between TRP and voltage-gated ion channels in their active states, and suggest a dual gating mechanism that may account for the ability of members of the TRP channel superfamily to integrate diverse physiological signals.

    • Erhu Cao
    • , Maofu Liao
    •  & David Julius

  • Article |

    A high-resolution electron cryo-microscopy structure of the rat transient receptor potential (TRP) channel TRPV1 in its ‘closed’ state is presented; the overall structure of this ion channel is found to share some common features with voltage-gated ion channels, although several unique, TRP-specific features are also characterized.

    • Maofu Liao
    • , Erhu Cao
    •  & Yifan Cheng

  • Article |

    X-ray crystal structures of a voltage-gated Na+channel mutated to be highly Ca2+selective provide a framework for understanding the mechanisms of ion selectivity and conductance in vertebrate voltage-gated Ca2+channels.

    • Lin Tang
    • , Tamer M. Gamal El-Din
    •  & William A. Catterall

  • Letter |

    A series of long molecular dynamics simulations shows that the K+ channel is sterically locked in the inactive conformation by buried water molecules bound behind the selectivity filter; a kinetic model deduced from the simulations shows how releasing the buried waters can elongate the timescale of the recovery period, and this hypothesis is confirmed using ‘wet’ biophysical experiments.

    • Jared Ostmeyer
    • , Sudha Chakrapani
    •  & Benoît Roux

  • 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

  • Article |

    Here it is shown that ion flux through the TrkH–TrkA complex is upregulated by ATP and downregulated by ADP; solving the X-ray crystal structures of the tetrameric TrkA ring in the absence and presence of TrkH suggests a mechanism by which ATP-induced conformational changes in TrkA augment the activity of TrkH.

    • Yu Cao
    • , Yaping Pan
    •  & Ming Zhou

  • Article |

    This study reports the X-ray crystal structure of a Ktr K+ transporter; the structure of this KtrAB complex reveals how the dimeric membrane protein KtrB interacts with the cytosolic octameric KtrA regulatory protein.

    • Ricardo S. Vieira-Pires
    • , Andras Szollosi
    •  & João H. Morais-Cabral

  • Letter |

    The crystal structure of the inner-membrane urea channel HpUreI from Helicobacter pylori, the causative organism of peptic ulcers, reveals how the channel selectively transports urea across the membrane and buffers the pathogen’s periplasmic pH against the acidic gastric environment.

    • David Strugatsky
    • , Reginald McNulty
    •  & Hartmut Luecke

  • Letter |

    A new class of peptides, mambalgins, is isolated from the African snake the black mamba, which can abolish pain through inhibition of particular subtypes of acid-sensing ion channels expressed either in central or peripheral neurons.

    • Sylvie Diochot
    • , Anne Baron
    •  & Eric Lingueglia

  • Article |

    Acid-sensing ion channels (ASICs) are voltage-independent ion channels that participate in a broad range of biological processes, including nociception and mechanosensation; here X-ray crystal structures of the complexes of chicken ASIC1a with psalmotoxin, a peptide toxin from tarantula, indicate that toxin binding triggers an expansion of the extracellular vestibule and stabilization of the open channel pore.

    • Isabelle Baconguis
    •  & Eric Gouaux

  • Letter |

    The crystal structure of NavRh, a NaChBac orthologue from the marine Rickettsiales sp. HIMB114, defines an ion binding site within the selectivity filter, and reveals several conformational rearrangements that may underlie the electromechanical coupling mechanism.

    • Xu Zhang
    • , Wenlin Ren
    •  & Nieng Yan

  • Letter |

    The voltage-gated calcium channel protein subunit α2δ is shown to control both the abundance of voltage-gated calcium channels and their coupling to the vesicular release of neurotransmitters into the synapse; because the α2δ family is a known target of potent analgesics, this study offers a new link between basic synaptic physiology and pain research in the clinic.

    • Michael B. Hoppa
    • , Beatrice Lana
    •  & Timothy A. Ryan

  • News & Views |

    Piezo proteins have been shown to form large ion channels that serve a sensory function in fruitflies. The findings help to explain how Piezos convert mechanical force into biological signals. See Article p.176 & Letter p.209

    • Philip A. Gottlieb
    •  & Frederick Sachs

  • Letter |

    Circadian rhythmicity of cardiac ion-channel expression and of an index of myocardial repolarization is under the control of Klf15, a clock-dependent oscillator that is required for generating transient outward potassium current, and deficiencies or excesses of which cause loss of rhythmic variation in myocardial and abnormal repolarization, and an enhanced susceptibility to ventricular arrhythmias.

    • Darwin Jeyaraj
    • , Saptarsi M. Haldar
    •  & Mukesh K. Jain

  • News & Views |

    When expressed in neurons, channelrhodopsin proteins allow the cells' electrical activity to be controlled by light. The structure of one such protein will guide efforts to make better tools for controlling neurons. See Article p.369

    • Oliver P. Ernst
    •  & Thomas P. Sakmar

  • Letter |

    STIM1-mediated gating of CRAC channels occurs through a mechanism in which ion selectivity and gating are closely coupled, and the residue V102 is identified as a candidate for the channel gate.

    • Beth A. McNally
    • , Agila Somasundaram
    •  & Murali Prakriya

  • Letter |

    The function of the KCNH family of potassium channels is critical for the repolarization of the cardiac action potential and the regulation of neuronal excitability; here, the X-ray crystal structure of the cyclic-nuclotide-binding homology domain of the zebrafish ELK channel is reported.

    • Tinatin I. Brelidze
    • , Anne E. Carlson
    •  & William N. Zagotta

  • Brief Communications Arising |

    • Taufiq Rahman
    • , Alexander Skupin
    •  & Colin W. Taylor

  • News & Views |

    Sodium channels in cell membranes have a crucial role in triggering bioelectrical events that lead to processes such as muscle contraction or hormone release. A crystal structure reveals how one such channel might work. See Article p.353

    • Richard Horn

  • Letter |

    Progesterone stimulates an increase in Ca2+ levels in human sperm, but the underlying signalling mechanism is poorly understood. Two studies now show that progesterone activates the sperm-specific, pH-sensitive CatSper calcium channel, leading to a rapid influx of Ca2+ ions into the spermatozoa. These results should help to define the physiological role of progesterone and CatSper in sperm, and could lead to the development of new classes of non-hormonal contraceptives.

    • Polina V. Lishko
    • , Inna L. Botchkina
    •  & Yuriy Kirichok

  • Letter |

    The mechanism of action of general anaesthetics is poorly understood, although there is some evidence that their principal protein targets are pentameric ligand-gated ion channels (pLGICs). Here, the X-ray crystal structures of propofol and desflurane bound to a bacterial homologue of the pLGIC family are solved. The structures reveal a common binding site for these two anaesthetics in the upper part of the transmembrane domain of each protomer.

    • Hugues Nury
    • , Catherine Van Renterghem
    •  & Pierre-Jean Corringer

  • Letter |

    Mutations in ryanodine receptors can lead to severe genetic conditions in both cardiac and skeletal muscles. These authors report the X-ray crystal structure of a type 1 ryanodine receptor and pinpoint the exact locations of more than 50 disease-related mutations in the full-length receptor. The disease mutations seem to cause misfolding of an individual domain, to destabilize interactions between the three amino-terminal domains, or to otherwise affect one of the other domain interfaces.

    • Ching-Chieh Tung
    • , Paolo A. Lobo
    •  & Filip Van Petegem

  • News & Views |

    The crystal structure of a protein channel provides clues about the mechanisms that control the closure of pores found in the epidermis of plant leaves. Excitingly, the protein channel folds in a way never seen before. See Article p.1074

    • Sébastien Thomine
    •  & Hélène Barbier-Brygoo

  • Article |

    SLAC1 is a plant ion channel that controls turgor pressure in the guard cells of plant stomata, thereby regulating the exchange of water vapour and photosynthetic gases in response to environmental signals. Here, the X-ray crystal structure of a bacterial homologue of SLAC1 has been solved, and structure-inspired mutagenesis has been used to analyse the conductance properties of the channel. The findings indicate that selectivity among different anions is largely a function of the energetic cost of ion dehydration.

    • Yu-hang Chen
    • , Lei Hu
    •  & Wayne A. Hendrickson

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