ArticleNature protocols2015
Proteome-wide identification of SUMO modification sites by mass spectrometry.
Article in Nature protocols, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 59 citations in OpenAlex.
- Understanding protein ISGylation, a multifaceted posttranslational modification.Cell chemical biology · 2026Review
- Organelle regulation of SUMOylation: regulatory mechanisms and therapeutic application.Journal of advanced research · 2026Review
- Characterization of endogenous SUMOylation sites by click chemistry-based proteomics.Analytical and bioanalytical chemistry · 2025Article
- Recent advances in proteomic workflows to interrogate the SUMOylome in plants.The New phytologist · 2025Review
- Substrate and Functional Diversity of Protein Lysine Post-translational Modifications.Genomics, proteomics & bioinformatics · 2024Review
- Rhes, a striatal enriched protein, regulates post-translational small-ubiquitin-like-modifier (SUMO) modification of nuclear proteins and alters gene expression.Cellular and molecular life sciences : CMLS · 2024Article
- SUMO modifies GβL and mediates mTOR signaling.The Journal of biological chemistry · 2024Article
- SUMOylation of AnxA6 facilitates EGFR-PKCα complex formation to suppress epithelial cancer growth.Cell communication and signaling : CCS · 2023Article
- Changes in SUMO-modified proteins in Epstein-Barr virus infection identifies reciprocal regulation of TRIM24/28/33 complexes and the lytic switch BZLF1.PLoS pathogens · 2023Article
- Function and regulation of ubiquitin-like SUMO system in heart.Frontiers in cell and developmental biology · 2023Review
- Pathological implication of protein post-translational modifications in cancer.Molecular aspects of medicine · 2022Review
- The Role of Protein SUMOylation in Human Hepatocellular Carcinoma: A Potential Target of New Drug Discovery and Development.Cancers · 2021Review
- The scaffold protein IQGAP1 links heat-induced stress signals to alternative splicing regulation in gastric cancer cells.Oncogene · 2021Article
- SUMO and Transcriptional Regulation: The Lessons of Large-Scale Proteomic, Modifomic and Genomic Studies.Molecules (Basel, Switzerland) · 2021Review
- SUMO is a pervasive regulator of meiosis.eLife · 2021Article
- Crosstalk Between SUMO and Ubiquitin-Like Proteins: Implication for Antiviral Defense.Frontiers in cell and developmental biology · 2021Review
- Proteomics Mapping of the ISGylation Landscape in Innate Immunity.Frontiers in immunology · 2021Review
- The Hydrogen-Coupled Oligopeptide Membrane Cotransporter Pept2 is SUMOylated in Kidney Distal Convoluted Tubule Cells.Frontiers in molecular biosciences · 2021Article
- SUMOylation in development and neurodegeneration.Development (Cambridge, England) · 2020Review
- The in vivo ISGylome links ISG15 to metabolic pathways and autophagy upon Listeria monocytogenes infection.Nature communications · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
The protein called 'small ubiquitin-like modifier' (SUMO) is post-translationally linked to target proteins at the ɛ-amino group of lysine residues. This 'SUMOylation' alters the behavior of the target protein, a change that is utilized to regulate diverse cellular processes. Understanding the target-specific consequences of SUMO modification requires knowledge of the location of conjugation sites, and we have developed a straightforward protocol for the proteome-wide identification of SUMO modification sites using mass spectrometry (MS). The approach described herein requires the expression of a mutant form of SUMO, in which the residue preceding the C-terminal Gly-Gly (diGly) is replaced with a lysine (SUMO(KGG)). Digestion of SUMO(KGG) protein conjugates with endoproteinase Lys-C yields a diGly motif attached to target lysines. Peptides containing this adduct are enriched using a diGly-Lys (K-ɛ-GG)-specific antibody and identified by MS. This diGly signature is characteristic of SUMO(KGG) conjugation alone, as no other ubiquitin-like protein (Ubl) yields this adduct upon Lys-C digestion. We have demonstrated the utility of the approach in SUMOylation studies, but, in principle, it may be adapted for the site-specific identification of proteins modified by any Ubl. Starting from cell lysis, this protocol can be completed in ∼5 d.
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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.