The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination
Open accessAbstract
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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In the citing paper
“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]
In the citing paper
“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]
Citations
Cites
1 retracted
Buschmann, T., Fuchs, S. Y., Lee, C.-G., Pan, Z., & Ronai, Z. A. (2000) · Cell · doi:10.1016/s0092-8674(00)80887-9 · Cited by 267
RetractedThe Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,296
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Hay, R. T. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.012 · Cited by 1,656
Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study
Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588
SUMO-1 Modification of IκBα Inhibits NF-κB Activation
Desterro, J. M. P., Rodríguez, M. S., & Hay, R. T. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80133-1 · Cited by 1,050
Alonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859
Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease
Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843
Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779
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Denver, G. H. (2016)
García‐Sierra, F. (2016) · Journal of Medical & Surgical Pathology · doi:10.4172/2472-4971.1000121
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Schaffert, L.-N., & Carter, W. G. (2021) · doi:10.1201/9781003180449-11
Horita, H. N., Law, A., & Middleton, K. M. (2018) · Journal of Visualized Experiments · doi:10.3791/56912-v
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Smith-Geater, C., Steffan, J. S., & Thompson, L. M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95672-7.00019-4
Nahar, M., Rai, R., Khan, A. G., & Jat, D. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-18716-2.00004-1
Liu, Y.-C., Hsu, W.-L., Ma, Y., Yin, C.-Y., Cheng, K.-M., & Lee, E. H. Y. (2025) · Molecular Medicine · doi:10.1186/s10020-025-01354-8
Ma, L., Herren, A. W., Espinal, G. M., Randol, J. L., McLaughlin, B. E., Martinez-Cerdeño, V., Pessah, I. N., Hagerman, R. J., & Hagerman, P. J. (2019) · Figshare · doi:10.6084/m9.figshare.9766562
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Gavilán, E. (2026) · Springer eBooks · doi:10.1007/978-981-95-6099-8_10
Schorova, L. (2018) · theses.fr (ABES) · doi:10.70675/a30a505az5e81z4089za24azcf43d27e33ce
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Despres, C. (2017) · theses.fr (ABES) · doi:10.70675/de10f843z8572z4295zb672z763dbf30e2b5
Yatoui, D. (2022) · theses.fr (ABES) · doi:10.70675/e3620ccez2ea7z43f2za0dcz257a72021b17
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Lee, J.-Y., Lee, J., Lee, S., Yoon, J. H., Park, D. G., & Sung, J. (2026) · medRxiv · doi:10.64898/2026.04.10.26350571
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颜亭祥, Vaquer, J., Springer, W., & Fiesel, F. C. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00031-2
Wang, R., Maloney, B., Nho, K. T., Beck, J. S., Counts, S., & Lahiri, D. K. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.11.731747
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Karthikeyan, K., & Chinnathambi, S. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2026.06.001
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Wu, Q., Fan, D., Ren, J., Xing, Y., Chen, Z., Jin, H., Lu, Y., Wang, X. R., & Zheng, H. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06050-0
Self-citationTau physiology and pathology: impacts on cellular structures and neurodegenerative diseases
Akbari, V., & Bahramikia, S. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02328-w
Therapeutic targeting of tauopathies: From druggable biology to precision intervention
Zhang, C., Ma, J., Wu, X., Wang, X., Huang, X., Zheng, H., & Zhao, Y. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108432
Self-citationZhang, J., Hu, H., Zhu, Y., 辛喜艳, 范瑞文, Ye, Y., & Li, D. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108464
Metadata
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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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