ArticleBMC biology2011
Sumo-dependent substrate targeting of the SUMO protease Ulp1.
Article in BMC biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- The role of SUMOylation in regulating proteins that drive neuronal disease progression.Biochemistry and biophysics reports · 2026Review
- Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery.Cell reports · 2026Article
- Identification and functional analysis of ULP2 SUMO protease mutants of the stress-tolerant yeastmicroPublication biology · 2025Article
- Article
- Genome sequencing and comparative genomics reveal insights into pathogenicity and evolution of Fusarium zanthoxyli, the causal agent of stem canker in prickly ash.BMC genomics · 2024Article
- Transient septin sumoylation steers a Fir1-Skt5 protein complex between the split septin ring.The Journal of cell biology · 2024Article
- Protein Modification Employing Non-Canonical Amino Acids to Prepare SUMOylation Detecting Bioconjugates.Pharmaceutics · 2022Article
- Chlamydomonas proteases: classification, phylogeny, and molecular mechanisms.Journal of experimental botany · 2021Article
- SUMO Protease SMT7 Modulates Ribosomal Protein L30 and Regulates Cell-Size Checkpoint Function.The Plant cell · 2020Article
- Recruitment of an Activated Gene to the Yeast Nuclear Pore Complex Requires Sumoylation.Frontiers in genetics · 2020Article
- SUMO-Chain-Regulated Proteasomal Degradation Timing Exemplified in DNA Replication Initiation.Molecular cell · 2019Article
- Recruitment of the Ulp2 protease to the inner kinetochore prevents its hyper-sumoylation to ensure accurate chromosome segregation.PLoS genetics · 2019Article
- Binding to small ubiquitin-like modifier and the nucleolar protein Csm1 regulates substrate specificity of the Ulp2 protease.The Journal of biological chemistry · 2018Article
- The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.Cytoskeleton (Hoboken, N.J.) · 2018Article
- SUMOylation regulates cytochrome P450 2E1 expression and activity in alcoholic liver disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- SUMO targeting of a stress-tolerant Ulp1 SUMO protease.PloS one · 2018Article
- Genome maintenance in Saccharomyces cerevisiae: the role of SUMO and SUMO-targeted ubiquitin ligases.Nucleic acids research · 2017Review
- Methionine adenosyltransferase α2 sumoylation positively regulate Bcl-2 expression in human colon and liver cancer cells.Oncotarget · 2015Article
- Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins.Cytoskeleton (Hoboken, N.J.) · 2015Review
- A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1.Molecular biology of the cell · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundIn the yeast Saccharomyces cerevisiae, the essential small ubiquitin-like modifier (SUMO) protease Ulp1 is responsible for both removing SUMO/Smt3 from specific target proteins and for processing precursor SUMO into its conjugation-competent form. Ulp1 localizes predominantly to nuclear pore complexes but has also been shown to deconjugate sumoylated septins at the bud-neck of dividing cells. How Ulp1 is directed to bud-neck localized septins and other cytoplasmic deconjugation targets is not well understood.
resultsUsing a structure/function approach, we set out to elucidate features of Ulp1 that are required for substrate targeting. To aid our studies, we took advantage of a catalytically inactive mutant of Ulp1 that is greatly enriched at the septin ring of dividing yeast cells. We found that the localization of Ulp1 to the septins requires both SUMO and specific structural features of Ulp1's catalytic domain. Our analysis identified a 218-amino acid, substrate-trapping mutant of the catalytic domain of Ulp1, Ulp1(3)(C580S), that is necessary and sufficient for septin localization. We also used the targeting and SUMO-binding properties of Ulp1(3)(C580S) to purify Smt3-modified proteins from cell extracts.
conclusionsOur study provides novel insights into how the Ulp1 SUMO protease is actively targeted to its substrates in vivo and in vitro. Furthermore, we found that a substrate-trapping Ulp1(3)(C580S) interacts robustly with human SUMO1, SUMO2 and SUMO2 chains, making it a potentially useful tool for the analysis and purification of SUMO-modified proteins.
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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.