S-Nitrosylation of Drp1 Mediates β-Amyloid-Related Mitochondrial Fission and Neuronal Injury
Open accessAbstract
Mitochondria continuously undergo two opposing processes, fission and fusion. The disruption of this dynamic equilibrium may herald cell injury or death and may contribute to developmental and neurodegenerative disorders. Nitric oxide functions as a signaling molecule, but in excess it mediates neuronal injury, in part via mitochondrial fission or fragmentation. However, the underlying mechanism for nitric oxide-induced pathological fission remains unclear. We found that nitric oxide produced in response to beta-amyloid protein, thought to be a key mediator of Alzheimer's disease, triggered mitochondrial fission, synaptic loss, and neuronal damage, in part via S-nitrosylation of dynamin-related protein 1 (forming SNO-Drp1). Preventing nitrosylation of Drp1 by cysteine mutation abrogated these neurotoxic events. SNO-Drp1 is increased in brains of human Alzheimer's disease patients and may thus contribute to the pathogenesis of neurodegeneration.
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Mitochondrial fission-fusion dynamics through alterations of Drp1, Parkin, and Pink1 functions are disrupted in various neurodegenerative diseases, including Parkinson's disease and Alzheimer's disease.
“Mitochondrial fission-fusion dynamics through alterations of Drp1, Parkin, and Pink1 functions (23,24), which play essential roles in mitophagy induction and mitochondrial quality control during healthy brain aging, are disrupted in various neurodegenerative diseases, including Parkinson’s disease (PD) and AD (25).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [23]
The paper’s Abstract links altered Drp1 activity and excessive mitochondrial fission to Alzheimer’s disease. It does not address Parkin or Pink1 functions or establish the broader claim across neurodegenerative diseases; its comparison of human brains found increased SNO-Drp1 in Alzheimer’s disease but not Parkinson’s disease. (LLM, conf=0.87)
Experimental — accuracy not yet measuredIncreased accumulation of APP and its processed peptides in mitochondria of AD neurons and effects on mitochondrial dynamics and mitophagy have been documented.
“Increased accumulation of APP and its processed peptides in the mitochondria of AD neurons and their effects on mitochondrial dynamics and mitophagy have been documented (21–24).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [23]
The passage labeled Abstract (page not provided) reports that Aβ promotes Drp1-mediated mitochondrial fission, supporting an effect on mitochondrial dynamics. It does not document accumulation of APP or its processed peptides inside mitochondria of AD neurons, or an effect on mitophagy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAβ-induced mitochondrial fission occurs in part because of the presence of Drp1 that has been S-nitrosylated, which enhances its fission activity.
“Aβ-induced mitochondrial fission occurs in part because of the presence of Drp1 that has been S-nitrosylated (a redox-related modification of cysteine thiol groups mediated by nitric oxide), which enhances its fission activity.”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Cho et al., 2009
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- Authors
- Cho, D.-H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., & Lipton, S. A.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Corresponding author
- Cho, Dong-Hyung
- Nakamura, Tomohiro
- Gu, Zezong
- Lipton, Stuart A.
- ORCID
- Venue
- Science
- Published
- 2009-04-03
- Volume
- 324
- Issue
- 5923
- Pages
- 102-105
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2823371
- OpenAlex
- W2085035881
- Cited by
- 1,092
- References
- 23
- Citations by year
- 2026: 29 · 2025: 40 · 2024: 55 · 2023: 57 · 2022: 48 · 2021: 85 · 2020: 66 · 2019: 42 · 2018: 64 · 2017: 63 · 2016: 70 · 2015: 58 · 2014: 68 · 2013: 76 · 2012: 87
- FWCI
- 36.14
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Eye Institute (R01 EY 05477, R01EY005477)
- National Institute of Neurological Disorders and Stroke (P30NS057096)
- National Institute of Environmental Health Sciences (P01ES016738)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P01HD29587, P01HD029587)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- S-nitrosylation, Drp1, mitochondrial fission, amyloid-beta, nitric oxide, Alzheimer's disease, neuronal injury, synaptic loss, mitochondrial dynamics, neurodegeneration, cysteine mutations
- MeSH terms
- Alzheimer Disease, Animals, Cell Line, Cerebral Cortex, Cysteine, Female, Humans, Male, Mice, Transgenic, Microtubule-Associated Proteins, Mitochondria, Models, Molecular, Mutation, Neurons, Nitric Oxide, Peptide Fragments, Amyloid beta-Peptides, Protein Structure, Tertiary, GTP Phosphohydrolases, Amino Acid Motifs, Mitochondrial Proteins, S-Nitrosothiols, Dynamins, Cell Line, Tumor, Mice, Protein Multimerization
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