Nuclear transport articles within Nature

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  • Article |

    Circular RNAs are exported from the nucleus by Ran-GTP, exportin-2 and IGF2BP1 in a mechanism analogous to protein export rather than mRNA export.

    • Linh H. Ngo
    • , Andrew G. Bert
    •  & Vihandha O. Wickramasinghe

  • Article |

    We report the cryo-electron microscopy structure of native pre-60S particles trapped in the channel of the yeast nuclear pore complex, suggesting a translocation model for the export of pre-60S particles through the complex.

    • Zongqiang Li
    • , Shuaijiabin Chen
    •  & Sen-Fang Sui

  • Article
    | Open Access

    Single-molecule calibrated live microscopy and computational modelling have revealed that human nuclear pore complex assembly takes different pathways during the exit from mitosis and during nuclear growth in interphase.

    • Shotaro Otsuka
    • , Jeremy O. B. Tempkin
    •  & Jan Ellenberg

  • Article |

    In-cell structural studies in Saccharomyces cerevisiae reveal that the configuration of the Nup159 complex is a key determinant of the mRNA export function of the nuclear pore complex, and suggest a model in which nuclear pore complexes are degraded via the autophagy machinery.

    • Matteo Allegretti
    • , Christian E. Zimmerli
    •  & Martin Beck

  • Article |

    The surfactant-like protein Ki-67 mediates the clustering of chromosomes during mitotic exit, which displaces large cytoplasmic molecules from the future nuclear space and thus enables the separation of cytoplasmic and nuclear components before the nuclear envelope reforms.

    • Sara Cuylen-Haering
    • , Mina Petrovic
    •  & Daniel W. Gerlich

  • Article |

    The structure of the yeast nuclear pore complex, determined at sub-nanometre precision using an integrative approach that combines a wide range of data, reveals details of its architecture, transport mechanism and evolutionary origins.

    • Seung Joong Kim
    • , Javier Fernandez-Martinez
    •  & Michael P. Rout

  • Letter |

    The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization.

    • Alexander von Appen
    • , Jan Kosinski
    •  & Martin Beck

  • Letter |

    BRCA2, the breast cancer susceptibility gene factor, interacts with TREX-2, a protein complex involved in the biogenesis and export of messenger ribonucleoprotein, to process DNA–RNA hybrid structures called R-loops that can trigger genome instability; these may be a central cause of the stress occurring in early cancer cells that drives oncogenesis.

    • Vaibhav Bhatia
    • , Sonia I. Barroso
    •  & Andrés Aguilera

  • Letter |

    Two proteins are identified in yeast that regulate the timing of pre-ribosome export from the nucleus; Nug2 binds pre-60S particles until they are ready for export, at which time Nug2 is replaced by the export adaptor Nmd3, enabling the export machinery to recognise the pre-ribosome that is ready to be transferred to the cytoplasm.

    • Yoshitaka Matsuo
    • , Sander Granneman
    •  & Ed Hurt

  • Article |

    The twin-arginine translocation (Tat) pathway transports folded proteins across membranes in bacteria and plant chloroplasts; the crystal structure of TatC, an integral membrane protein and core component of this complex, is now presented.

    • Sarah E. Rollauer
    • , Michael J. Tarry
    •  & Susan M. Lea

  • Letter |

    Newly synthesized messenger RNA is exported from the nucleus through nuclear pores. Here, a new imaging and tracking method has been developed to study the kinetics of mRNA export, with 20-ms time-precision and 26-nm spatial precision. A three-step model for export is presented, comprising docking, transport and release. Notably, mRNAs can move bi-directionally through the pore complex.

    • David Grünwald
    •  & Robert H. Singer

  • Letter |

    Nuclear pore complexes selectively transport cargos across the nuclear envelope. Here, a nuclear transport assay has been developed that allows the movement of single cargo proteins to be followed in real time. A succession of transport substeps is observed, and the NPC is found to be functionally asymmetric to importing cargos. The study provides insight into the mechanism of selective transport through the NPC.

    • Alan R. Lowe
    • , Jake J. Siegel
    •  & Jan T. Liphardt

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