Ginkgolic Acid Inhibits Protein SUMOylation by Blocking Formation of the E1-SUMO Intermediate
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Protein modification by small ubiquitin-related modifier proteins (SUMOs) controls diverse cellular functions. Dysregulation of SUMOylation or deSUMOylation processes has been implicated in the development of cancer and neurodegenerative diseases. However, no small-molecule inhibiting protein SUMOylation has been reported so far. Here, we report inhibition of SUMOylation by ginkgolic acid and its analog, anacardic acid. Ginkgolic acid and anacardic acid inhibit protein SUMOylation both in vitro and in vivo without affecting in vivo ubiquitination. Binding assays with a fluorescently labeled probe showed that ginkgolic acid directly binds E1 and inhibits the formation of the E1-SUMO intermediate. These studies will provide not only a useful tool for investigating the roles of SUMO conjugations in a variety of pathways in cells, but also a basis for the development of drugs targeted against diseases involving aberrant SUMOylation.
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Anacardic acid, an inhibitor of protein SUMOylation, abrogated pksC E. coli-induced senescence.
“Furthermore, the use of anacardic acid, an inhibitor of protein SUMOylation, 16 abrogated pksC E. coliinduced senescence (unpublished data).”
From The bacterial genotoxin colibactin promotes colon tumor growth by modifying the tumor microenvironment (2014) · cites this paper as [16]
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SUMOylation Represses Nanog Expression via Modulating Transcription Factors Oct4 and Sox2
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Natural Salicylates and Their Roles in Human Health
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SUMO targets the APC/C to regulate transition from metaphase to anaphase
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Small molecules for mesenchymal stem cell fate determination
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The emerging roles of SUMOylation in the tumor microenvironment and therapeutic implications
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Along the Central Dogma—Controlling Gene Expression with Small Molecules
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- Authors
- Fukuda, I., Ito, A., Hirai, G., Nishimura, S., Kawasaki, H., Saitoh, H., Kimura, K.-I., Sodeoka, M., & Yoshida, M.
- Affiliations
- RIKEN Advanced Science Institute (JP)
- Japan Science and Technology Agency (JP)
- RIKEN (JP)
- Tokyo Denki University (JP)
- Institute of Molecular Embryology and Genetics, Kumamoto University (JP)
- Iwate University (JP)
- Corresponding author
- Ito, Akihiro
- ORCID
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 16
- Issue
- 2
- Pages
- 133-140
- ISSN
- 1074-5521 (ISSN-L)
- OpenAlex
- W1978693761
- Cited by
- 355
- References
- 23
- Citations by year
- 2026: 14 · 2025: 23 · 2024: 25 · 2023: 23 · 2022: 21 · 2021: 27 · 2020: 28 · 2019: 27 · 2018: 31 · 2017: 30 · 2016: 23 · 2015: 20 · 2014: 31 · 2013: 9 · 2012: 6
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Chemistry & Biology (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Sakura: Saitama United Cyber Repository of Academic Resources (Saitama University) (submittedVersion)
- Funders
- Core Research for Evolutional Science and Technology
- Advanced Science Institute
- Japan Science and Technology Corporation
- Ministry of Education, Culture, Sports, Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- ginkgolic acid, anacardic acid, protein sumoylation, SUMOylation inhibition, small molecule inhibitors, SUMO conjugation, ubiquitination, drug development
- MeSH terms
- Plant Extracts, Protein Binding, Salicylates, Structure-Activity Relationship, Plant Leaves, Ginkgo biloba, Small Ubiquitin-Related Modifier Proteins, Anacardic Acids, Small Molecule Libraries, Ubiquitination
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