Nuclear pore complex

The nuclear pore complex mediates the selective exchange of components, including RNA, ribosomal proteins, signalling molecules and lipids between the nucleus and the cytoplasm. It is one of the largest protein complexes in the cells. Small molecules diffuse through them while larger molecules are recognised by specific components called nucleoporins to be transported through the pores.

Latest Research and Reviews

  • Research | | open

    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
    • , Dana Rinaldi
    • , Jean-Yves Dauxois
    •  & Pierre-Emmanuel Gleizes
  • Research | | open

    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
    • , Sahradha Albert
    • , Miroslava Schaffer
    • , Daniela Strenkert
    • , Patrice A. Salomé
    • , Sabeeha S. Merchant
    • , Jürgen M. Plitzko
    • , Wolfgang Baumeister
    • , Benjamin D. Engel
    •  & Martin Beck
  • Research | | open

    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
    • , Sarah W. Cai
    • , Ferdinand M. Huber
    • , Claudia A. Jette
    •  & André Hoelz
  • Research | | open

    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
    • , Alex Tuck
    • , Bertrand Cosson
    • , Frédéric Devaux
    •  & Benoit Palancade
  • Research |

    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
    • , Ilona Nudelman
    • , Yi Shi
    • , Wenzhu Zhang
    • , Barak Raveh
    • , Thurston Herricks
    • , Brian D. Slaughter
    • , Joanna A. Hogan
    • , Paula Upla
    • , Ilan E. Chemmama
    • , Riccardo Pellarin
    • , Ignacia Echeverria
    • , Manjunatha Shivaraju
    • , Azraa S. Chaudhury
    • , Junjie Wang
    • , Rosemary Williams
    • , Jay R. Unruh
    • , Charles H. Greenberg
    • , Erica Y. Jacobs
    • , Zhiheng Yu
    • , M. Jason de la Cruz
    • , Roxana Mironska
    • , David L. Stokes
    • , John D. Aitchison
    • , Martin F. Jarrold
    • , Jennifer L. Gerton
    • , Steven J. Ludtke
    • , Christopher W. Akey
    • , Brian T. Chait
    • , Andrej Sali
    •  & Michael P. Rout
    Nature 555, 475-482

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