Nuclear pore complex articles within Nature Communications

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  • Article
    | Open Access

    There is little information on export directionality of RNA passing through the nuclear pore complex in human cells. Here, the authors examine single RNA molecules in transit, to demonstrate 5’-first directionality for the export of mRNA and lncRNA.

    • Asaf Ashkenazy-Titelman
    • , Mohammad Khaled Atrash
    •  & Yaron Shav-Tal

  • Article
    | Open Access

    The biogenesis of nuclear pores imposes a logistic challenge for cells. Here, the authors investigate structural motifs for co-translational interactions in nucleoporins and find that co-translational assembly events differ between paralogous assembly pathways thus contributing to faithful assembly.

    • Maximilian Seidel
    • , Anja Becker
    •  & Martin Beck

  • Article
    | Open Access

    The Y complex is an essential component of the nuclear pore complex but a full model based on experimental structures is lacking. Here, the authors complete the model of the yeast Y complex with two nanobody-bound crystal structures, providing molecular insights into its flexibility and membrane anchoring.

    • Sarah A. Nordeen
    • , Daniel L. Turman
    •  & Thomas U. Schwartz

  • Article
    | Open Access

    The contribution of central and peripheral channels of nuclear pores to transport of transmembrane proteins is unclear. Here the authors show that most inner nuclear membrane proteins use only peripheral channels, but some extend nuclear localization signals into the central channel for directed nuclear transport.

    • Krishna C. Mudumbi
    • , Rafal Czapiewski
    •  & Weidong Yang

  • Article
    | Open Access

    The nuclear pore complex (NPC) is known to regulate p53 signaling and this has mainly been linked to peripheral NPC subunits. Here the authors show that Nup155 from the NPC inner ring regulates the p53 pathway by controlling p21 translation while also being a target of p53-mediated repression.

    • Kerstin Holzer
    • , Alessandro Ori
    •  & Stephan Singer

  • Article
    | Open Access

    Large protein complexes and ribonucleoprotein particles (RNPs) such as pre-ribosomes are transported from the nucleus to the cytoplasm through the nuclear pore complex (NPC). Here the authors use ultrafast freezing and electron tomography to catch snapshots of native RNPs crossing the NPC and estimate their transit time using a probabilistic model.

    • Franck Delavoie
    • , Vanessa Soldan
    •  & Pierre-Emmanuel Gleizes

  • Article
    | Open Access

    While the architecture of vertebrate nuclear pore complexes (NPCs) is well understood, the extent of its evolutionary conservation is still unclear. Here, the authors analyze the in situ architecture of an algal NPC, revealing distinct structural features that provide insights into NPC evolution.

    • Shyamal Mosalaganti
    • , Jan Kosinski
    •  & Martin Beck

  • Article
    | Open Access

    The export of mRNA to the cytosol depends on the nuclear pore complex (NPC) and the activation of the helicase DDX19, but their interplay in humans remains poorly understood. Here, the authors present a structural and functional analysis of DDX19 activation, revealing how the human NPC regulates mRNA export.

    • Daniel H. Lin
    • , Ana R. Correia
    •  & André Hoelz

  • Article
    | Open Access

    The nuclear pore complex is crucial for mediating nucleocytoplasmic exchanges. Here the authors use budding yeast to reveal a mechanism responsible of maintaining nucleoporin homeostasis by sensing changes in the complex integrity and further altering the metabolism of the corresponding mRNAs.

    • Jérôme O. Rouvière
    • , Manuel Bulfoni
    •  & Benoit Palancade

  • Article
    | Open Access

    The proteome-wide characterization of proteostasis depends on robust approaches to determine protein half-lives. Here, the authors improve the accuracy and precision of mass spectrometry-based quantification, enabling reliable protein half-life determination in several non-dividing cell types.

    • Toby Mathieson
    • , Holger Franken
    •  & Mikhail M. Savitski

  • Article
    | Open Access

    Measuring single-cell mRNA dynamics is critical to understand gene expression. Here, using RNA Spinach technique to detect very low abundant mRNAs, Guet et al. report an analysis of the osmotic shock response in live yeast by localizing induced transcription factors, target gene loci and corresponding transcripts.

    • David Guet
    • , Laura T. Burns
    •  & Catherine Dargemont

  • Article
    | Open Access

    Nuclear pore complexes (NPCs) are large macromolecular assemblies that mediate the exchange of molecules between the nucleus and cytoplasm. Here the authors present a ∼20 Å cryo-EM structure of the X. laevisNPC in different states of transport to propose a model for the architecture of the NPC’s molecular gate within its central channel.

    • Matthias Eibauer
    • , Mauro Pellanda
    •  & Ohad Medalia

  • Article
    | Open Access

    Retroviruses such as HIV integrate into the host genome as an essential step prior to their replication. Here Lelek et al. identify nuclear pore complex proteins that are essential for HIV nuclear import and productive integration, and show that the intranuclear protein Tpr influences integration into transcriptionally active chromatin.

    • Mickaël Lelek
    • , Nicoletta Casartelli
    •  & Francesca Di Nunzio

  • Article
    | Open Access

    TFIID is an essential transcription factor complex that controls the expression of most protein-coding genes in eukaryotes. Here the authors identify and characterize a complex containing TAF2, TAF8 and TAF10, which assembles in the cytoplasm before integration into the nuclear holo–TFIID complex.

    • Simon Trowitzsch
    • , Cristina Viola
    •  & Imre Berger

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