Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (586 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
A type of post-translational protein modification by small ubiquitin-related modifier proteins (also known as SUMO proteins).
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Sumoylations; SUMO-Conjugation; SUMO Conjugation; SUMO-Conjugations.
Where it fits in the MeSH classification
- Broader topics
- Ubiquitination
Related concepts
- Post-Translational Protein Modification
- Small Ubiquitin-Related Modifier Proteins
Research landscape
PubMed indexes 3,270 records tagged with the MeSH heading “Sumoylation” (counts retrieved 2026-10-29). 1,313 of them (40.2%) were published from 2020 onward, and the busiest period so far is 2010-2019 with 1,984 records.
Reviews account for 490 records (15.0%) and meta-analyses for 0. Randomized controlled trials number 0 (0.0%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 0 |
| 2000-2009 | 1 |
| 2010-2019 | 1,984 |
| 2020 onward | 1,313 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 490 | 15.0% |
| Meta-analyses | 0 | 0.0% |
| Randomized controlled trials | 0 | 0.0% |
Method: PubMed query "Sumoylation"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-29.
Reading the evidence in molecular biology
Molecular biology establishes mechanisms through controlled experiments, often in simplified systems such as purified proteins, cultured cells or model organisms. Such work can show what is possible in a defined system, but whether a pathway matters in a whole organism or in human disease needs further evidence. Check the experimental system, whether findings were reproduced by independent groups, and whether the authors tested the mechanism directly or inferred it from correlation.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| TRIM28 SUMOylates and stabilizes NLRP3 to facilitate inflammasome activation | 2021 | Research article Design not recorded in structured metadata | 146 | cc by PMID 34373456 · DOI · PMC8352945 |
| Histone sumoylation and chromatin dynamics | 2021 | Review article Design not recorded in structured metadata | 128 | cc by PMID 33885816 · DOI · PMC8216275 |
| SUMOylation modification-mediated cell death | 2021 | Review article Design not recorded in structured metadata | 91 | cc by PMID 34255975 · DOI · PMC8277462 |
| Ubc9-Mediated SUMOylation of RPL3, an Unappreciated Mechanism against Hepatocyte Senescence by Repressing the DHX9-p16 Axis | 2026 | Research article Design not recorded in structured metadata | 2 | cc by PMID 41114463 · DOI · PMC12767081 |
TRIM28 SUMOylates and stabilizes NLRP3 to facilitate inflammasome activation [1]
Abstract reading summary — source excerpts
- Opening excerpt
- The cellular NLRP3 protein level is crucial for assembly and activation of the NLRP3 inflammasome.
- Closing excerpt
- These data identify a mechanism by which SUMOylation controls the cellular NLRP3 level and inflammasome activation, and reveal correlations and interactions of NLRP3 SUMOylation and ubiquitination during inflammasome activation.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (136 words)
The cellular NLRP3 protein level is crucial for assembly and activation of the NLRP3 inflammasome. Various posttranslational modifications (PTMs), including phosphorylation and ubiquitination, control NLRP3 protein degradation and inflammasome activation; however, the function of small ubiquitin-like modifier (SUMO) modification (called SUMOylation) in controlling NLRP3 stability and subsequent inflammasome activation is unclear. Here, we show that the E3 SUMO ligase tripartite motif-containing protein 28 (TRIM28) is an enhancer of NLRP3 inflammasome activation by facilitating NLRP3 expression. TRIM28 binds NLRP3, promotes SUMO1, SUMO2 and SUMO3 modification of NLRP3, and thereby inhibits NLRP3 ubiquitination and proteasomal degradation. Concordantly, Trim28 deficiency attenuates NLRP3 inflammasome activation both in vitro and in vivo. These data identify a mechanism by which SUMOylation controls the cellular NLRP3 level and inflammasome activation, and reveal correlations and interactions of NLRP3 SUMOylation and ubiquitination during inflammasome activation.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 34373456 · DOI · PMC8352945
Histone sumoylation and chromatin dynamics [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Chromatin structure and gene expression are dynamically controlled by post-translational modifications (PTMs) on histone proteins, including ubiquitylation, methylation, acetylation and small ubiquitin-like modifier (SUMO) conjugation.
- Closing excerpt
- This review describes recent findings on histone sumoylation and its coordination with other histone and RNAPII-CTD modifications in the regulation of chromatin dynamics.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (131 words)
Chromatin structure and gene expression are dynamically controlled by post-translational modifications (PTMs) on histone proteins, including ubiquitylation, methylation, acetylation and small ubiquitin-like modifier (SUMO) conjugation. It was initially thought that histone sumoylation exclusively suppressed gene transcription, but recent advances in proteomics and genomics have uncovered its diverse functions in cotranscriptional processes, including chromatin remodeling, transcript elongation, and blocking cryptic initiation. Histone sumoylation is integral to complex signaling codes that prime additional histone PTMs as well as modifications of the RNA polymerase II carboxy-terminal domain (RNAPII-CTD) during transcription. In addition, sumoylation of histone variants is critical for the DNA double-strand break (DSB) response and for chromosome segregation during mitosis. This review describes recent findings on histone sumoylation and its coordination with other histone and RNAPII-CTD modifications in the regulation of chromatin dynamics.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 33885816 · DOI · PMC8216275
SUMOylation modification-mediated cell death [3]
Abstract reading summary — source excerpts
- Opening excerpt
- SUMOylation dynamically conjugates SUMO molecules to the lysine residue of a substrate protein, which depends on the physiological state of the cell and the attached SUMO isoforms.
- Closing excerpt
- Mapping the exact SUMOylation network with cellular death contributes to develop novel SUMOylation-targeting disease therapeutic strategies.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (130 words)
SUMOylation dynamically conjugates SUMO molecules to the lysine residue of a substrate protein, which depends on the physiological state of the cell and the attached SUMO isoforms. A prominent role of SUMOylation in molecular pathways is to govern the cellular death process. Herein, we summarize the association between SUMOylation modification events and four types of cellular death processes: apoptosis, autophagy, senescence and pyroptosis. SUMOylation positively or negatively regulates a certain cellular death pattern depending on specific conditions including the attached SUMO isoforms, disease types, substrate proteins and cell context. Moreover, we also discuss the possible role of SUMOylation in ferroptosis and propose a potential role of the SUMOylated GPX4 in the regulation of ferroptosis. Mapping the exact SUMOylation network with cellular death contributes to develop novel SUMOylation-targeting disease therapeutic strategies.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 34255975 · DOI · PMC8277462
Ubc9-Mediated SUMOylation of RPL3, an Unappreciated Mechanism against Hepatocyte Senescence by Repressing the DHX9-p16 Axis [4]
Abstract reading summary — source excerpts
- Opening excerpt
- Although Ubc9-mediated SUMOylation are recognized to regulate the multiple aspects of hepatic biological processes, its impact on hepatic senescence and metabolic dysfunction-associated steatotic liver disease (MASLD), however, is yet to be fully addressed.
- Closing excerpt
- Together, the study highlights that Ubc9-mediated SUMOylation of RPL3 could be an unappreciated mechanism against hepatic aging in clinical settings.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (189 words)
Although Ubc9-mediated SUMOylation are recognized to regulate the multiple aspects of hepatic biological processes, its impact on hepatic senescence and metabolic dysfunction-associated steatotic liver disease (MASLD), however, is yet to be fully addressed. Herein noted an age-dependent decrease of hepatic Ubc9 expression is first noted along with an escalated decrease of protein SUMOylation, which is coupled with enhanced senescent marker expressions both in humans and mice. Interestingly, Ubc9 is dispensable for liver development at the embryonic stage. However, Ubc9 deficiency in hepatocytes rendered mice with an exacerbated hepatic aging phenotype and more susceptible to fatty liver disease and steatohepatitis following the challenge of a methionine- and choline-deficient (MCD)-diet. Ii is further demonstrated that nuclear ribosomal protein L3 (RPL3) interacts with DExD/H-box (DDX/DHX) helicases (DHX9), which then recruits RNA polymerase II to the p16 promoter to transcribe its expression, thereby exacerbating the hepatocyte aging process. However, Ubc9-mediated SUMOylation prevents RPL3 nuclear translocation, by which it represses the expression of senescent markers such as p16 to attenuate the hepatic aging process. Together, the study highlights that Ubc9-mediated SUMOylation of RPL3 could be an unappreciated mechanism against hepatic aging in clinical settings.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41114463 · DOI · PMC12767081
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Sumoylation: a regulatory protein modification in health and disease [5]
- Research article Signalling mechanisms and cellular functions of SUMO [6]
- Research article The post-translational modification, SUMOylation, and cancer (Review) [7]
- Research article SUMOylation-Mediated Regulation of Cell Cycle Progression and Cancer [8]
- Research article SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes [9]
- Research article SUMO conjugation - a mechanistic view [10]
References
- Qin Y, Li Q, Liang W, Yan R, Tong L, Jia M, et al.. TRIM28 SUMOylates and stabilizes NLRP3 to facilitate inflammasome activation. . 2021. PMID 34373456 · DOI · PMC8352945
- Ryu HY, Hochstrasser M. Histone sumoylation and chromatin dynamics. . 2021. PMID 33885816 · DOI · PMC8216275
- Sheng Z, Zhu J, Deng YN, Gao S, Liang S. SUMOylation modification-mediated cell death. . 2021. PMID 34255975 · DOI · PMC8277462
- Xie H, Gao Z, Liu X, Zhang S, Wang Y, Gao J, et al.. Ubc9-Mediated SUMOylation of RPL3, an Unappreciated Mechanism against Hepatocyte Senescence by Repressing the DHX9-p16 Axis. . 2026. PMID 41114463 · DOI · PMC12767081
- Flotho A, Melchior F. Sumoylation: a regulatory protein modification in health and disease. Annu Rev Biochem. 2013. PMID 23746258 · DOI
- Vertegaal ACO. Signalling mechanisms and cellular functions of SUMO. Nat Rev Mol Cell Biol. 2022. PMID 35750927 · DOI
- Han ZJ, Feng YH, Gu BH, Li YM, Chen H. The post-translational modification, SUMOylation, and cancer (Review). Int J Oncol. 2018. PMID 29484374 · DOI · PMC5843405
- Eifler K, Vertegaal ACO. SUMOylation-Mediated Regulation of Cell Cycle Progression and Cancer. Trends Biochem Sci. 2015. PMID 26601932 · DOI · PMC4874464
- Zhao X. SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes. Mol Cell. 2018. PMID 30075142 · DOI · PMC6095470
- Pichler A, Fatouros C, Lee H, Eisenhardt N. SUMO conjugation - a mechanistic view. Biomol Concepts. 2017. PMID 28284030 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-29.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.