Cited by 237Alzheimer's disease research and treatmentsUbiquitin and proteasome pathwaysDementia and Cognitive Impairment Research

SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination

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Luo, Hong-Bin, Xia, Yi-Yuan, Shu, Xi-Ji, Liu, Zan-Chao, Feng, Ye, Liu, Xing-Hua, Yu, Guang, Yin, Gang +6 more·2014·Proceedings of the National Academy of Sciences

Abstract

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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Crossref · 10.1073/pnas.1417548111

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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
Published
2014-11-05
Volume
111
Issue
46
Pages
16586-16591
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
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
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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