Posttranslational marks control architectural and functional plasticity of the nuclear pore complex basket

The Journal of Cell Biology
Carlos A NiñoCatherine Dargemont

Abstract

The nuclear pore complex (NPC) serves as both the unique gate between the nucleus and the cytoplasm and a major platform that coordinates nucleocytoplasmic exchanges, gene expression, and genome integrity. To understand how the NPC integrates these functional constraints, we dissected here the posttranslational modifications of the nuclear basket protein Nup60 and analyzed how they intervene to control the plasticity of the NPC. Combined approaches highlight the role of monoubiquitylation in regulating the association dynamics of Nup60 and its partner, Nup2, with the NPC through an interaction with Nup84, a component of the Y complex. Although major nuclear transport routes are not regulated by Nup60 modifications, monoubiquitylation of Nup60 is stimulated upon genotoxic stress and regulates the DNA-damage response and telomere repair. Together, these data reveal an original mechanism contributing to the plasticity of the NPC at a molecular-organization and functional level.

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Sep 8, 2016·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Hicham Saad, Jennifer A Cobb
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Jun 3, 2021·International Journal of Molecular Sciences·Ya-Chu ChangAnja-Katrin Bielinsky

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Methods Mentioned

BETA
electron microscopy
fluorescence recovery
ubiquitination
flow cytometry
PCR
immunoprecipitation
sumoylation

Software Mentioned

iLas
Genevust
ImageJ
TurboReg
MetaMorph

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