ArticlePLoS genetics2017
A high throughput mutagenic analysis of yeast sumo structure and function.
Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Non-covalent SUMO interactions with ligases and effectors: SUMO-interacting motifs and beyond.Essays in biochemistry · 2025Review
- PolySUMOylation of PCNA and Rad52 restricts centromeric recombination in fission yeast.Nature communications · 2025Article
- Growth inhibition of Saccharomyces cerevisiae by SUMO-specific nanobodies.Scientific reports · 2025Article
- The SUMO gene MrSmt3 is involved in SUMOylation, conidiation and stress response in Metarhizium robertsii.Scientific reports · 2024Article
- Article
- 1,10-phenanthroline inhibits sumoylation and reveals that yeast SUMO modifications are highly transient.EMBO reports · 2024Article
- Article
- Paralogue-Specific Roles of SUMO1 and SUMO2/3 in Protein Quality Control and Associated Diseases.Cells · 2023Review
- The Ubiquitin-like Proteins ofBiomolecules · 2023Review
- Zinc controls PML nuclear body formation through regulation of a paralog specific auto-inhibition in SUMO1.Nucleic acids research · 2022Article
- Implications of critical node-dependent unidirectional cross-talk of Plasmodium SUMO pathway proteins.Biophysical journal · 2022Article
- SUMO Interacting Motifs: Structure and Function.Cells · 2021Review
- SUMO paralogue-specific functions revealed through systematic analysis of human knockout cell lines and gene expression data.Molecular biology of the cell · 2021Article
- Nucleolar release of rDNA repeats for repair involves SUMO-mediated untethering by the Cdc48/p97 segregase.Nature communications · 2021Article
- Acetylation of SUMO2 at lysine 11 favors the formation of non-canonical SUMO chains.EMBO reports · 2018Article
- The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.Cytoskeleton (Hoboken, N.J.) · 2018Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Sumoylation regulates a wide range of essential cellular functions through diverse mechanisms that remain to be fully understood. Using S. cerevisiae, a model organism with a single essential SUMO gene (SMT3), we developed a library of >250 mutant strains with single or multiple amino acid substitutions of surface or core residues in the Smt3 protein. By screening this library using plate-based assays, we have generated a comprehensive structure-function based map of Smt3, revealing essential amino acid residues and residues critical for function under a variety of genotoxic and proteotoxic stress conditions. Functionally important residues mapped to surfaces affecting Smt3 precursor processing and deconjugation from protein substrates, covalent conjugation to protein substrates, and non-covalent interactions with E3 ligases and downstream effector proteins containing SUMO-interacting motifs. Lysine residues potentially involved in formation of polymeric chains were also investigated, revealing critical roles for polymeric chains, but redundancy in specific chain linkages. Collectively, our findings provide important insights into the molecular basis of signaling through sumoylation. Moreover, the library of Smt3 mutants represents a valuable resource for further exploring the functions of sumoylation in cellular stress response and other SUMO-dependent pathways.
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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.