MFN2 couples glutamate excitotoxicity and mitochondrial dysfunction in motor neurons
Open accessAbstract
Mitochondrial dysfunction plays a central role in glutamate-evoked neuronal excitotoxicity, and mitochondrial fission/fusion dynamics are essential for mitochondrial morphology and function. Here, we establish a novel mechanistic linker among glutamate excitotoxicity, mitochondrial dynamics, and mitochondrial dysfunction in spinal cord motor neurons. Ca 2+ -dependent activation of the cysteine protease calpain in response to glutamate results in the degradation of a key mitochondrial outer membrane fusion regulator, mitofusin 2 (MFN2), and leads to MFN2-mediated mitochondrial fragmentation preceding glutamate-induced neuronal death. MFN2 deficiency impairs mitochondrial function, induces motor neuronal death, and renders motor neurons vulnerable to glutamate excitotoxicity. Conversely, MFN2 overexpression blocks glutamate-induced mitochondrial fragmentation, mitochondrial dysfunction, and/or neuronal death in spinal cord motor neurons both in vitro and in mice. The inhibition of calpain activation also alleviates glutamate-induced excitotoxicity of mitochondria and neurons. Overall, these results suggest that glutamate excitotoxicity causes mitochondrial dysfunction by impairing mitochondrial dynamics via calpain-mediated MFN2 degradation in motor neurons and thus present a molecular mechanism coupling glutamate excitotoxicity and mitochondrial dysfunction.Mitochondrial function is dependent on mitochondrial fission and fusion dynamics. Results Calpain-mediated degradation of MFN2 is responsible for glutamate-induced mitochondrial dysfunction and neuronal death in spinal cord motor neurons. Conclusion Calpain-mediated MFN2 degradation is a novel mechanism regulating mitochondrial fusion during glutamate excitotoxicity. Significance MFN2 might be a novel therapeutic target against glutamate excitotoxicity in motor neurons.
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Ferroptosis may operate through damage other than mitochondrial cellular membranes, such as the cytoplasmic membrane.
“This aligns with the knowledge that mitochondrial dysfunction is characteristic of the excitotoxic pathway (Nicholls and Budd, 1998; Votyakova and Reynolds, 2005), whereas ferroptosis may operate through damage other than (Wang et al., 2015) mitochondrial cellular membranes, such as the cytoplasmic membrane (Vaglio-Garro et al., 2024b).”
From Toxic Concentrations of Glutamate Induce Ferroptosis without Affecting Mitochondrial Respiration in Rodent Brain Slice Cultures (2026) · cites this paper as Wang et al., 2015
The Abstract and Discussion describe mitochondrial fragmentation and dysfunction during glutamate excitotoxicity in motor neurons. Our copy does not address whether ferroptosis damages cytoplasmic rather than mitochondrial membranes; searches for ferroptosis and membrane damage found no passage supporting that comparison. (LLM, conf=0.78)
Experimental — accuracy not yet measuredIncreased mitochondrial fragmentation precedes glutamate-induced death of motor neurons.
“increased mitochondrial fragmentation has been found to precede glutamate-induced death of motor neurons (143).”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [143]
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- Authors
- Wang, W., Zhang, F., Li, L., Tang, F., Siedlak, S. L., Fujioka, H., Liu, Y., Su, B., Pi, Y., & Wang, X.
- Affiliations
- Case Western Reserve University (US)
- Shandong University (CN)
- Corresponding author
- Wang, Xinglong
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2015-01
- Volume
- 290
- Issue
- 1
- Pages
- 168-182
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4281719
- OpenAlex
- W1986005605
- Cited by
- 103
- References
- 67
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 7 · 2023: 6 · 2022: 12 · 2021: 15 · 2020: 9 · 2019: 14 · 2018: 13 · 2017: 5 · 2016: 9 · 2015: 6
- FWCI
- 2.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (R03AG044680, R21NS085747, R01NS089604)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- mitofusin 2, glutamate excitotoxicity, mitochondrial dysfunction, mitochondrial fission, mitochondrial fusion, calpain, motor neurons, neuronal cell death, spinal cord, mitochondrial fragmentation, protein degradation
- MeSH terms
- Animals, Calcium, Calpain, Embryo, Mammalian, Female, Gene Expression Regulation, Male, Membrane Proteins, Mice, Transgenic, Mitochondria, Motor Neurons, Spinal Cord, Signal Transduction, Cell Death, Rats, Sprague-Dawley, Glutamic Acid, GTP Phosphohydrolases, Mitochondrial Proteins, Mice, Rats, Proteolysis, Primary Cell Culture, Mitochondrial Dynamics
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