Membrane biophysics articles within Nature

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  • Article
    | Open Access

    High-speed molecular tracking is integrated with three-dimensional electron microscopy to map the diffusion distribution and ultrastructure of endoplasmic reticulum-mitochondria contact sites, revealing the ability of high-speed single-molecule imaging to map contact site interface structures and corresponding diffusion landscapes.

    • Christopher J. Obara
    • , Jonathon Nixon-Abell
    •  & Jennifer Lippincott-Schwartz

  • 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 |

    A theoretical model, in vitro reconstitution and in vivo experimentation show that competition between droplet surface tension and membrane sheet instability dictates the form and function of autophagosomal membranes.

    • Jaime Agudo-Canalejo
    • , Sebastian W. Schultz
    •  & Roland L. Knorr

  • 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 |

    Solvent contrast modulation reveals how the lipid bilayer actively participates in the conformational switches of Ca2+-ATPase through the actions of tryptophan, arginine and lysine residues, which function as membrane floats and anchors.

    • Yoshiyuki Norimatsu
    • , Kazuya Hasegawa
    •  & Chikashi Toyoshima

  • 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 |

    Super-resolution imaging provides direct evidence in live cells that membrane fusion and fission are mediated through an intermediate hemi-fused structure, where fusion and calcium/dynamin-dependent fission mechanisms compete to determine the transition of the intermediate to fusion or fission.

    • Wei-Dong Zhao
    • , Edaeni Hamid
    •  & Ling-Gang Wu

  • Letter |

    Although several X-ray crystal structures of G protein-coupled receptors (GPCRs) have been reported, relatively little is known about the conformational dynamics of these important membrane proteins; here, the authors used NMR spectroscopy to monitor the conformational changes that occur in the turkey β1-adrenergic receptor in the presence of antagonists, partial agonists, and full agonists.

    • Shin Isogai
    • , Xavier Deupi
    •  & Stephan Grzesiek

  • Letter |

    Fluorescent labelling is used to show that in E. coli, outer membrane protein (OMP) turnover is passive and binary in nature, and OMPs cluster to form islands in which diffusion of individual proteins is restricted owing to lateral interactions with other OMPs; new OMPs are inserted mostly at mid-cell, meaning that old OMP islands are displaced to the poles of growing cells.

    • Patrice Rassam
    • , Nikki A. Copeland
    •  & Colin Kleanthous

  • Brief Communications Arising |

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

  • Article |

    Metastatic cancer cells are shown to have a tendency towards forming a bulky glycocalyx owing to the production of large glycoproteins, and this cancer-associated glycocalyx has a mechanical effect on the spatial organization of integrins — by funnelling integrins into adhesions, integrin clustering and signalling is promoted, which leads to enhanced cell survival and proliferation.

    • Matthew J. Paszek
    • , Christopher C. DuFort
    •  & Valerie M. Weaver

  • 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 crystal structure of a nucleotide-free energy-coupling factor transporter from Lactobacillus brevis at a resolution of 3.5 Å suggests a plausible working model for the transport cycle of such transporters.

    • Tingliang Wang
    • , Guobin Fu
    •  & Yigong Shi

  • 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

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