ArticleCell reports2024
The polySUMOylation axis promotes nucleolar release of Tof2 for mitotic exit.
Article in Cell reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- More than SAM: mechanisms of action of the Polycomb group protein polyhomeotic.Nucleus (Austin, Tex.) · 2026Review
- Role of Nuclear SUMO-Targeted Ubiquitin Ligase Uls2 (Slx5-Slx8) in Quality Control of Cytosolic Proteins.Biomolecules · 2026Article
- Cdc5-mediated Ulp2 phosphorylation controls the timing of polySUMOylation during the cell cycle.The Journal of cell biology · 2026Article
- PolySUMOylation of PCNA and Rad52 restricts centromeric recombination in fission yeast.Nature communications · 2025Article
- Regulation of misfolded protein aggregation and degradation by SUMOylation in budding yeast.Molecular biology of the cell · 2025Article
- Significance of SUMOylation in breast cancer progression: a comprehensive investigation using single-cell analysis and bioinformatics.Frontiers in immunology · 2025Article
- The role of SUMOylation in biomolecular condensate dynamics and protein localization.Cell insight · 2024Review
- Decoding the Nucleolar Role in Meiotic Recombination and Cell Cycle Control: Insights into Cdc14 Function.International journal of molecular sciences · 2024Review
- Machine Learning Modelling, Single-Cell Landscape Profiling and Spatial Transcriptomics Provide New Insights Into SUMOylation in Head and Neck Squamous Cell Carcinoma.IET systems biologyArticle
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Authors and funding
6 authors.
Funding
Abstract
In budding yeast, the nucleolus serves as the site to sequester Cdc14, a phosphatase essential for mitotic exit. Nucleolar proteins Tof2, Net1, and Fob1 are required for this sequestration. Although it is known that these nucleolar proteins are SUMOylated, how SUMOylation regulates their activity remains unknown. Here, we show that Tof2 exhibits cell-cycle-regulated nucleolar delocalization and turnover. Depletion of the nuclear small ubiquitin-like modifier (SUMO) protease Ulp2 not only causes Tof2 polySUMOylation, nucleolar delocalization, and degradation but also leads to Cdc14 nucleolar release and activation. This outcome depends on polySUMOylation and the activity of downstream enzymes, including SUMO-targeted ubiquitin ligase and Cdc48/p97 segregase. We further developed a system to tether SUMO machinery to Tof2 and generated a SUMO-deficient tof2 mutant, and the results indicate that Tof2 polySUMOylation is necessary and sufficient for its nucleolar delocalization and degradation. Together, our work reveals a polySUMO-dependent mechanism that delocalizes Tof2 from the nucleolus to facilitate mitotic exit.
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