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

    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
    • , Amy Cooke
    • , Daniel Dauch
    • , Elisabeth Drucker
    • , Philip Riemenschneider
    • , Amparo Andres-Pons
    • , Amanda L. DiGuilio
    • , Marie-Therese Mackmull
    • , Jochen Baßler
    • , Stephanie Roessler
    • , Kai Breuhahn
    • , Lars Zender
    • , Joseph S. Glavy
    • , Frank Dombrowski
    • , Ed Hurt
    • , Peter Schirmacher
    • , Martin Beck
    •  & Stephan Singer
  • 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

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