Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

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. © 2016 Niño et al.


Carlos A Niño, David Guet, Alexandre Gay, Sergine Brutus, Frédéric Jourquin, Shweta Mendiratta, Jean Salamero, Vincent Géli, Catherine Dargemont. Posttranslational marks control architectural and functional plasticity of the nuclear pore complex basket. The Journal of cell biology. 2016 Jan 18;212(2):167-80

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 26783300

View Full Text