SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination
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Significance: Intracellular accumulation of the abnormally modified tau is hallmark pathology of AD, but the mechanism leading to tau aggregation is not fully characterized. In the present study, we studied the effects of tau SUMOylation on its phosphorylation, ubiquitination, degradation, and aggregation. We discovered that sumoylation competes with ubiquitination in modifying tau, correlating with tau hyperphosphorylation. Identification of the posttranslational modification on tau provides the new insight into the molecular mechanism in tau aggregation.
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SUMO1 immunoreactivity was found to correlate with phosphorylated tau in AD patient brain.
“Tau sumoylation may be pathogenic, as SUMO1 immunoreactivity was found to correlate with phosphorylated tau in AD patient brain.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [173]
Sumoylation enhances tau phosphorylation, but reduces tau ubiquitination and UPS-mediated degradation.
“Sumoylation enhances tau phosphorylation, but reduces tau ubiquitination and UPS-mediated degradation [173].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [173]
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Self-citation
- Authors
- Luo, H.-B., Xia, Y.-Y., Shu, X.-J., Liu, Z.-C., Feng, Y., Liu, X.-H., Yu, G., Yin, G., Xiong, Y.-S., Zeng, K., Jiang, J., Ye, K., Wang, X.-C., & Wang, J.-Z.
- Affiliations
- Department of Pathophysiology, School of Basic Medicine, Key Laboratory of Ministry of Education of China for Neurological Disorders, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China;
- Department of Pathology and Pathophysiology, School of Medicine, Jianghan University, Wuhan 430056, China;
- Huazhong University of Science and Technology (CN)
- Emory University (US)
- Nantong University (CN)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-11-05
- Volume
- 111
- Issue
- 46
- Pages
- 16586-16591
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4246270
- OpenAlex
- W1996406602
- Cited by
- 236
- References
- 56
- Citations by year
- 2026: 18 · 2025: 22 · 2024: 23 · 2023: 23 · 2022: 21 · 2021: 30 · 2020: 19 · 2019: 15 · 2018: 22 · 2017: 20 · 2016: 13 · 2015: 10
- FWCI
- 9.56
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (NSFC) (81271405)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau hyperphosphorylation, tau degradation, Alzheimer's disease, SUMO1, ginkgolic acid, amyloid-beta, tau aggregation, hippocampal neurons, cerebral cortex
- MeSH terms
- Glycogen Synthase Kinase 3 beta, Wortmannin, Alzheimer Disease, Androstadienes, Animals, Cerebral Cortex, Female, Hippocampus, Humans, Indoles, Male, Maleimides, Middle Aged, Nerve Tissue Proteins, Peptide Fragments, Phosphorylation, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Salicylates, Solubility, Amyloid beta-Peptides, Mutagenesis, Site-Directed, tau Proteins, Rats, Sprague-Dawley, Point Mutation, Amino Acid Substitution, Mutation, Missense, SUMO-1 Protein, Glycogen Synthase Kinase 3, Proteasome Endopeptidase Complex, Rats, Ubiquitination, HEK293 Cells, Sumoylation, Proteolysis
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