The function of SUMOylation and its crucial roles in the development of neurological diseases
Abstract
Neurological diseases are relatively complex diseases of a large system; however, the detailed mechanism of their pathogenesis has not been completely elucidated, and effective treatment methods are still lacking for some of the diseases. The SUMO (small ubiquitin-like modifier) modification is a dynamic and reversible process that is catalyzed by SUMO-specific E1, E2, and E3 ligases and reversed by a family of SENPs (SUMO/Sentrin-specific proteases). SUMOylation covalently conjugates numerous cellular proteins, and affects their cellular localization and biological activity in numerous cellular processes. A wide range of neuronal proteins have been identified as SUMO substrates, and the disruption of SUMOylation results in defects in synaptic plasticity, neuronal excitability, and neuronal stress responses. SUMOylation disorders cause many neurodegenerative diseases, such as Parkinson's disease, Alzheimer's disease, and Huntington's disease. By modulating the ion channel subunit, SUMOylation imbalance is responsible for the development of various channelopathies. The regulation of protein SUMOylation in neurons may provide a new strategy for the development of targeted therapeutic drugs for neurodegenerative diseases and channelopathies.
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SUMO1 is a useful AD marker whose expression level in plasma is tightly associated with AD pathology.
“Included were AD-related gene COPA, a gene that can reduce amyloid plaques in the cortex and hippocampus of the AD mouse models (58), and SUMO1, a useful AD marker whose expression level in plasma is tightly associated with AD pathology (59).”
From Comprehensive characterization of the transcriptional landscape in Alzheimer’s disease (AD) brains (2025) · cites this paper as [59]
Cites
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829 · see citing works
Protein misfolding in the endoplasmic reticulum as a conduit to human disease
Wang, M., & Kaufman, R. J. (2016) · Nature · doi:10.1038/nature17041 · Cited by 1,630 · see citing works
The bowel and beyond: The enteric nervous system in neurological disorders
Rao, M., & Gershon, M. D. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.107 · Cited by 629 · see citing works
Tau phosphorylation in neuronal cell function and dysfunction
Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624 · see citing works
The Promise of Minocycline in Neurology
Yong, V. W., Wells, J., Giuliani, F., Casha, S., Power, C., & Metz, L. M. (2004) · The Lancet Neurology · doi:10.1016/s1474-4422(04)00937-8 · Cited by 518 · see citing works
SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
David, G., Neptune, M. A., & DePinho, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203690200 · Cited by 236 · see citing works
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., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417548111 · Cited by 236 · see citing works
Ochaba, J., Monteys, A. M., O’Rourke, J. G., Reidling, J. C., Steffan, J. S., Davidson, B. L., & Thompson, L. M. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.016 · Cited by 94 · see citing works
Endres, K., & Schäfer, K.-H. (2018) · Journal of Innate Immunity · doi:10.1159/000488629 · Cited by 52 · see citing works
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Comprehensive characterization of the transcriptional landscape in Alzheimer’s disease (AD) brains
Chen, C., Zhang, Z., Liu, Y., Hong, W., Karahan, H., Wang, J., Li, W., Diao, L., Yu, M., Saykin, A. J., et al. (2025) · Science Advances · doi:10.1126/sciadv.adn1927 · Cited by 6 · see citing works
“Included were AD-related gene COPA , a gene that can reduce amyloid plaques in the cortex and hippocampus of the AD mouse models ( 58 ), and SUMO1 , a useful AD marker whose expression level in plasma is tightly associated with AD pathology ( 59 ).”
- Authors
- Chen, X., Zhang, Y., Wang, Q., Qin, Y., Yang, X., Xing, Z., Shen, Y., Wu, H., & Qi, Y.
- Affiliations
- Shaanxi Normal University (CN)
- Corresponding author
- Wu, Hongmei
- Qi, Yitao
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2021-03-12
- Volume
- 35
- Issue
- 4
- Pages
- e21510-e21510
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W3135165479
- Cited by
- 39
- References
- 9
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 7 · 2023: 9 · 2022: 8 · 2021: 2
- FWCI
- 0.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81671294, 81870241)
- Fundamental Research Funds for the Central Universities (GK201903066)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Keywords
- SUMOylation, SUMO, neurological disorders, neurodegenerative diseases, Parkinson's disease, Alzheimer's disease, Huntington's disease, channelopathies, ion channels, SUMO E3 ligase, synaptic plasticity, neuronal excitability, neuronal stress response
- MeSH terms
- Animals, Humans, Nervous System Diseases, Endopeptidases, Protein Processing, Post-Translational, Small Ubiquitin-Related Modifier Proteins, SUMO-1 Protein, Sumoylation
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