ArticleThe Journal of biological chemistry2015
Pli1(PIAS1) SUMO ligase protected by the nuclear pore-associated SUMO protease Ulp1SENP1/2.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery.Cell reports · 2026Article
- Ulp1 association with nuclear pore complexes is required for the maintenance of global SUMOylation.Molecular biology of the cell · 2025Article
- Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.PLoS biology · 2025Article
- SUMO protease and proteasome recruitment at the nuclear periphery differently affect replication dynamics at arrested forks.Nucleic acids research · 2024Article
- SUMOylation regulates Lem2 function in centromere clustering and silencing.Journal of cell science · 2023Article
- Review
- SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability.International journal of molecular sciences · 2021Review
- The nuclear pore primes recombination-dependent DNA synthesis at arrested forks by promoting SUMO removal.Nature communications · 2020Article
- The role of SUMOylation during development.Biochemical Society transactions · 2020Review
- Asymmetrical localization of Nup107-160 subcomplex components within the nuclear pore complex in fission yeast.PLoS genetics · 2019Article
- SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes.Molecular cell · 2018Review
- SUMO targeting of a stress-tolerant Ulp1 SUMO protease.PloS one · 2018Article
- A reference-based protein degradation assay without global translation inhibitors.The Journal of biological chemistry · 2017Article
- The STUbL RNF4 regulates protein group SUMOylation by targeting the SUMO conjugation machinery.Nature communications · 2017Article
- SUMO-targeted ubiquitin ligase activity can either suppress or promote genome instability, depending on the nature of the DNA lesion.PLoS genetics · 2017Article
- Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity.Genes & development · 2017Article
- Functional Crosstalk between the PP2A and SUMO Pathways Revealed by Analysis of STUbL Suppressor, razor 1-1.PLoS genetics · 2016Article
- Cooperativity of the SUMO and Ubiquitin Pathways in Genome Stability.Biomolecules · 2016Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Covalent modification of the proteome by SUMO is critical for genetic stability and cell growth. Equally crucial to these processes is the removal of SUMO from its targets by the Ulp1 (HuSENP1/2) family of SUMO proteases. Ulp1 activity is normally spatially restricted, because it is localized to the nuclear periphery via interactions with the nuclear pore. Delocalization of Ulp1 causes DNA damage and cell cycle defects, phenotypes thought to be caused by inappropriate desumoylation of nucleoplasmic targets that are normally spatially protected from Ulp1. Here, we define a novel consequence of Ulp1 deregulation, with a major impact on SUMO pathway function. In fission yeast lacking Nup132 (Sc/HuNUP133), Ulp1 is delocalized and can no longer antagonize sumoylation of the PIAS family SUMO E3 ligase, Pli1. Consequently, SUMO chain-modified Pli1 is targeted for proteasomal degradation by the concerted action of a SUMO-targeted ubiquitin ligase (STUbL) and Cdc48-Ufd1-Npl4. Pli1 degradation causes the profound SUMO pathway defects and associated centromere dysfunction in cells lacking Nup132. Thus, perhaps counterintuitively, Ulp1-mediated desumoylation can promote SUMO modification by stabilizing a SUMO E3 ligase.
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