ArticleGenome research2013
Genome-wide bimolecular fluorescence complementation analysis of SUMO interactome in yeast.
Article in Genome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- AP-3 and the V-ATPase modulate CTP synthase assembly through spatial association at the yeast vacuole.Molecular biology of the cell · 2026Article
- AP-3 and the V-ATPase Modulate CTP Synthase Assembly Through Spatial Association at the Yeast Vacuole.bioRxiv : the preprint server for biology · 2026Article
- A comprehensive overview of yeast libraries and their role in advancing cell biology.The FEBS journal · 2026Review
- Clu1/Clu form mitochondria-associated granules upon metabolic transitions and regulate mitochondrial protein translation via ribosome interactions.PLoS genetics · 2025Article
- Ulp1 association with nuclear pore complexes is required for the maintenance of global SUMOylation.Molecular biology of the cell · 2025Article
- A Live Cell Protein Complementation Assay for ORFeome-Wide Probing of Human HOX Interactomes.Cells · 2023Article
- A Yeast BiFC-seq Method for Genome-wide Interactome Mapping.Genomics, proteomics & bioinformatics · 2022Article
- Identification of proximal SUMO-dependent interactors using SUMO-ID.Nature communications · 2021Article
- Selective functional inhibition of a tumor-derived p53 mutant by cytosolic chaperones identified using split-YFP in budding yeast.G3 (Bethesda, Md.) · 2021Article
- Protein-fragment complementation assays for large-scale analysis of protein-protein interactions.Biochemical Society transactions · 2021Review
- Analysis of the TORC1 interactome reveals a spatially distinct function of TORC1 in mRNP complexes.The Journal of cell biology · 2021Article
- mRNA display with library of even-distribution reveals cellular interactors of influenza virus NS1.Nature communications · 2020Article
- Super-resolution Microscopy-based Bimolecular Fluorescence Complementation to Study Protein Complex Assembly and Co-localization.Bio-protocol · 2020Article
- Protein Topology Prediction Algorithms Systematically Investigated in the Yeast Saccharomyces cerevisiae.BioEssays : news and reviews in molecular, cellular and developmental biology · 2019Article
- Article
- Genome-Wide Studies of Rho5-Interacting Proteins That Are Involved in Oxidant-Induced Cell Death in Budding Yeast.G3 (Bethesda, Md.) · 2019Article
- Global analysis of protein homomerization inGenome research · 2019Article
- Generation of a versatile BiFC ORFeome library for analyzing protein-protein interactions in liveeLife · 2018Article
- The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.Cytoskeleton (Hoboken, N.J.) · 2018Article
- A genetic screen to discover SUMOylated proteins in living mammalian cells.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The definition of protein-protein interactions (PPIs) in the natural cellular context is essential for properly understanding various biological processes. So far, however, most large-scale PPI analyses have not been performed in the natural cellular context. Here, we describe the construction of a Saccharomyces cerevisiae fusion library in which each endogenous gene is C-terminally tagged with the N-terminal fragment of Venus (VN) for a genome-wide bimolecular fluorescence complementation assay, a powerful technique for identifying PPIs in living cells. We illustrate the utility of the VN fusion library by systematically analyzing the interactome of the small ubiquitin-related modifier (SUMO) and provide previously unavailable information on the subcellular localization, types, and protease dependence of SUMO interactions. Our data set is highly complementary to the existing data sets and represents a useful resource for expanding the understanding of the physiological roles of SUMO. In addition, the VN fusion library provides a useful research tool that makes it feasible to systematically analyze PPIs in the natural cellular context.
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