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J Cell Sci ; 132(7)2019 04 03.
Article in English | MEDLINE | ID: mdl-30837289

ABSTRACT

The nuclear pore complex (NPC) is the major conduit for nucleocytoplasmic transport and serves as a platform for gene regulation and DNA repair. Several nucleoporins undergo ubiquitylation and SUMOylation, and these modifications play an important role in nuclear pore dynamics and plasticity. Here, we perform a detailed analysis of these post-translational modifications of yeast nuclear basket proteins under normal growth conditions as well as upon cellular stresses, with a focus on SUMOylation. We find that the balance between the dynamics of SUMOylation and deSUMOylation of Nup60 and Nup2 at the NPC differs substantially, particularly in G1 and S phase. While Nup60 is the unique target of genotoxic stress within the nuclear basket that probably belongs to the SUMO-mediated DNA damage response pathway, both Nup2 and Nup60 show a dramatic increase in SUMOylation upon osmotic stress, with Nup2 SUMOylation being enhanced in Nup60 SUMO-deficient mutant yeast strains. Taken together, our data reveal that there are several levels of crosstalk between nucleoporins, and that the post-translational modifications of the NPC serve in sensing cellular stress signals.


Subject(s)
Cysteine Endopeptidases/metabolism , Nuclear Pore Complex Proteins/metabolism , Nuclear Pore/metabolism , Saccharomyces cerevisiae Proteins/metabolism , Sumoylation , Active Transport, Cell Nucleus , Cysteine Endopeptidases/chemistry , Cysteine Endopeptidases/genetics , DNA Repair , Nuclear Pore/ultrastructure , Nuclear Pore Complex Proteins/genetics , Protein Processing, Post-Translational , Saccharomyces cerevisiae/cytology , Saccharomyces cerevisiae/metabolism , Saccharomyces cerevisiae Proteins/genetics
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