ArticleThe Journal of cell biology2003
The Ulp1 SUMO isopeptidase: distinct domains required for viability, nuclear envelope localization, and substrate specificity.
Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
105 citing papers in PubMed, 194 citations in OpenAlex.
- Comparative Analysis of Lifecycle-Dependent A to I RNA Editing in Three Members of theJournal of fungi (Basel, Switzerland) · 2026Article
- Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery.Cell reports · 2026Article
- Cdc5-mediated Ulp2 phosphorylation controls the timing of polySUMOylation during the cell cycle.The Journal of cell biology · 2026Article
- Recombinant Production and Characterization of Human Enzymes Responsible for Collagen Lysine Post-translational Modifications.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Article
- Putative type III effector SkP48 of Bradyrhizobium sp. DOA9 encoding a SUMO protease blocks nodulation in Vigna radiata.Scientific reports · 2025Article
- Growth inhibition of Saccharomyces cerevisiae by SUMO-specific nanobodies.Scientific reports · 2025Article
- Identification and functional analysis of ULP2 SUMO protease mutants of the stress-tolerant yeastmicroPublication biology · 2025Article
- A miniature low-immunogenic platform for the biosynthesis of self-assembling protein nanoparticles.Nanotheranostics · 2025Article
- The role of SUMOylation in biomolecular condensate dynamics and protein localization.Cell insight · 2024Review
- Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024Review
- SUMOylation of rice DELLA SLR1 modulates transcriptional responses and improves yield under salt stress.Planta · 2024Article
- Article
- SUMOylation regulates Lem2 function in centromere clustering and silencing.Journal of cell science · 2023Article
- Article
- A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription.PLoS genetics · 2021Article
- SUMO is a pervasive regulator of meiosis.eLife · 2021Article
- Multiple Domains in the Rhizobial Type III Effector Bel2-5 Determine Symbiotic Efficiency With Soybean.Frontiers in plant science · 2021Article
- CiBER-seq dissects genetic networks by quantitative CRISPRi profiling of expression phenotypes.Science (New York, N.Y.) · 2020Article
- The necessity of NEDD8/Rub1 for vitality and its association with mitochondria-derived oxidative stress.Redox biology · 2020Review
45 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein modification by the ubiquitin-like SUMO protein contributes to many cellular regulatory mechanisms. In Saccharomyces cerevisiae, both sumoylating and desumoylating activities are essential for viability. Of its two known desumoylating enzymes, Ubl-specific protease (Ulp)1 and Ulp2/Smt4, Ulp1 is specifically required for cell cycle progression. A approximately 200-residue segment, the Ulp domain (UD), is conserved among Ulps and includes a core cysteine protease domain that is even more widespread. Here we demonstrate that the Ulp1 UD by itself can support wild-type growth rates and in vitro can cleave SUMO from substrates. However, in cells expressing only the UD of Ulp1, many SUMO conjugates accumulate to high levels, indicating that the nonessential Ulp1 NH2-terminal domain is important for activity against a substantial fraction of sumoylated targets. The NH2-terminal domain also includes sequences necessary and sufficient to concentrate Ulp1 at nuclear envelope sites. Remarkably, NH2-terminally deleted Ulp1 variants are able, unlike full-length Ulp1, to suppress defects of cells lacking the divergent Ulp2 isopeptidase. Thus, the NH2-terminal regulatory domain of Ulp1 restricts Ulp1 activity toward certain sumoylated proteins while enabling the cleavage of others. These data define key functional elements of Ulp1 and strongly suggest that subcellular localization is a physiologically significant constraint on SUMO isopeptidase specificity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.