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A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits

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Dokumenter

DOI

  • Jérôme O. Rouvière
  • Manuel Bulfoni, Université Paris—Denis Diderot
  • ,
  • Alex Tuck, University of Edinburgh, Wellcome Trust Centre for Cell Biology, Friedrich Miescher Institute for Biomedical Research
  • ,
  • Bertrand Cosson, Université Paris—Denis Diderot
  • ,
  • Frédéric Devaux, LOCEAN Laboratory
  • ,
  • Benoit Palancade, Université Paris—Denis Diderot

While the activity of multiprotein complexes is crucial for cellular metabolism, little is known about the mechanisms that collectively control the expression of their components. Here, we investigate the regulations targeting the biogenesis of the nuclear pore complex (NPC), the macromolecular assembly mediating nucleocytoplasmic exchanges. Systematic analysis of RNA-binding proteins interactomes, together with in vivo and in vitro assays, reveal that a subset of NPC mRNAs are specifically bound by Hek2, a yeast hnRNP K-like protein. Hek2-dependent translational repression and protein turnover are further shown to finely tune the levels of NPC subunits. Strikingly, mutations or physiological perturbations altering pore integrity decrease the levels of the NPC-associated SUMO protease Ulp1, and trigger the accumulation of sumoylated versions of Hek2 unable to bind NPC mRNAs. Our results support the existence of a quality control mechanism involving Ulp1 as a sensor of NPC integrity and Hek2 as a repressor of NPC biogenesis.

OriginalsprogEngelsk
Artikelnummer1665
TidsskriftNature Communications
Vol/bind9
Antal sider13
ISSN2041-1723
DOI
StatusUdgivet - 25 apr. 2018

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