Mitochondrial Dynamics is an important component in the neurobiology of neurodegenerative [diseases[/[diseases[/[diseases[/[diseases[/[diseases[/[diseases[/[diseases[/[diseases[/diseases. This page provides detailed information about its structure, function, and role in disease processes.
Mitochondrial dynamics refers to the continuous, opposing processes of mitochondrial fusion and fission that regulate mitochondrial morphology, distribution, quality control, and function. These processes are governed by large GTPase [proteins[/[proteins[/[proteins[/[proteins[/[proteins[/[proteins[/[proteins[/[proteins[/proteins — Mitofusin 1/2 (MFN1/2) and OPA1 for fusion, and [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- with its receptors for fission. In [neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons--TEMP--/entities)--FIX--, which have extraordinary metabolic demands and highly polarized morphologies (axons extending >1 meter in motor [neurons), mitochondrial dynamics are essential for distributing functional mitochondria to synapses, maintaining bioenergetic competence, and clearing damaged organelles through [mitophagy[/mechanisms/[mitophagy[/mechanisms/[mitophagy[/mechanisms/[mitophagy[/mechanisms/[mitophagy--TEMP--/mechanisms)--FIX--.
Disrupted mitochondrial dynamics — typically manifesting as excessive fragmentation (fission > fusion) — is a convergent pathological feature across virtually all neurodegenerative diseases, including [Alzheimer's disease[/diseases/[alzheimers[/diseases/[alzheimers[/diseases/[alzheimers[/diseases/[alzheimers--TEMP--/diseases)--FIX--, [Parkinson's disease[/diseases/[parkinsons[/diseases/[parkinsons[/diseases/[parkinsons[/diseases/[parkinsons--TEMP--/diseases)--FIX--, [Huntington's disease[/mechanisms/[huntington-pathway[/mechanisms/[huntington-pathway[/mechanisms/[huntington-pathway[/mechanisms/[huntington-pathway--TEMP--/mechanisms)--FIX--, [ALS[/diseases/[als[/diseases/[als[/diseases/[als[/diseases/[als--TEMP--/diseases)--FIX--, and [Charcot-Marie-Tooth Disease[/diseases/[charcot-marie-tooth-disease[/diseases/[charcot-marie-tooth-disease[/diseases/[charcot-marie-tooth-disease[/diseases/[charcot-marie-tooth-disease--TEMP--/diseases)--FIX--. Genetic evidence directly linking fusion/fission machinery to neurodegeneration includes MFN2 mutations (CMT2A), OPA1 mutations (autosomal dominant optic atrophy), and DNM1L ([DRP1) mutations causing lethal encephalopathy (Detmer & Chan, 2007; Bertholet et al., 2016).
Fusion is a two-step process mediated by three dynamin-related GTPases that merge the outer and inner mitochondrial membranes sequentially:
¶ Outer Membrane Fusion: Mitofusins (MFN1 and MFN2)
| Feature |
MFN1 |
MFN2 |
| Location |
Outer mitochondrial membrane |
Outer mitochondrial membrane; also ER/MAM |
| GTPase activity |
Higher (more efficient fusion) |
Lower; compensated by tethering function |
| ER-mito tethering |
Minimal role |
Major role; MFN2 on ER tethers to MFN1/2 on mitochondria |
| Disease mutations |
Not linked to human disease |
>100 mutations cause CMT2A (axonal neuropathy) |
| Expression |
Ubiquitous |
Enriched in heart, skeletal muscle, brain |
Mitofusins are anchored in the outer membrane with two transmembrane domains, presenting both N-terminal GTPase and C-terminal heptad repeat domains to the cytosol. Fusion occurs when MFN proteins on adjacent mitochondria form homo- or heterotypic dimers in trans, bringing outer membranes into proximity. GTP hydrolysis drives conformational changes that overcome the energy barrier to membrane merger (Chen & Chan, 2009).
MFN2 has an additional critical function at mitochondria-associated ER membranes (MAMs): it bridges ER and mitochondria, enabling calcium transfer (via IP3R-VDAC-MCU axis) and phospholipid exchange. Disruption of this tethering function contributes to neurodegeneration independently of its fusion role.
OPA1 is an inner mitochondrial membrane GTPase that mediates inner membrane fusion and cristae remodeling:
- Long forms (L-OPA1): Membrane-anchored; mediate inner membrane fusion
- Short forms (S-OPA1): Soluble; generated by proteolytic processing (OMA1 and YME1L proteases); involved in cristae remodeling
- Cristae junction maintenance: OPA1 oligomers maintain tight cristae junctions, preventing cytochrome c release; disruption triggers [apoptosis[/entities/[apoptosis[/entities/[apoptosis[/entities/[apoptosis[/entities/[apoptosis--TEMP--/entities)--FIX--
- Disease: >400 OPA1 mutations cause autosomal dominant optic atrophy (ADOA/Kjer's disease), the most common inherited optic neuropathy, through selective degeneration of retinal ganglion cells
The balance between L-OPA1 and S-OPA1 is dynamically regulated: mitochondrial stress, membrane depolarization, or ATP depletion triggers OMA1-mediated cleavage of L-OPA1 to S-OPA1, inhibiting fusion and promoting fission of damaged mitochondria.
[DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- is the central GTPase mediating mitochondrial fission. It is recruited from the cytosol to the outer mitochondrial membrane by receptor proteins:
| Receptor |
Role |
| MFF |
Primary receptor for physiological fission; directly activates [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- GTPase |
| MiD49/MiD51 |
Recruit and nucleate [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- oligomers; may sequester [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- in inactive state |
| FIS1 |
Primarily mediates stress-induced/pathological fission; key target for therapeutic inhibition |
[DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- assembles into contractile rings (16–24 monomers) around the mitochondrial constriction point — typically at ER-mitochondria contact sites where the ER has already pre-constricted the mitochondrial tubule to ~150 nm. GTP hydrolysis drives ring constriction to ~50 nm, followed by final scission.
Post-translational regulation of [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- is critical:
- Ser616 phosphorylation (Cdk1, ERK, CaMKII): Activates fission
- Ser637 phosphorylation (PKA): Inhibits fission
- S-nitrosylation (Cys644): Activates fission; elevated in AD brain
- SUMOylation: Promotes mitochondrial localization
A key discovery was that fission occurs preferentially at sites where the endoplasmic reticulum contacts mitochondria. ER tubules wrap around mitochondria and pre-constrict them before [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- recruitment. This ER-mediated constriction is essential because [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- rings cannot constrict mitochondria from their normal ~300–500 nm diameter; the ER narrows them to ~150 nm, within the range of [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- ring assembly (Friedman et al., 2011).
¶ Spatial Regulation and Energy Demands
Neuronal mitochondria must be positioned with precision:
| Location |
Mitochondrial Function |
Regulation |
| Synaptic terminals |
ATP for vesicle cycling, Ca[2]⁺ buffering |
Activity-dependent; halted by syntaphilin anchoring |
| Axonal branch points |
Regional energy supply |
[DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX---mediated fission generates small, mobile mitochondria |
| Nodes of Ranvier |
Na⁺/K⁺-ATPase function |
Stationary mitochondrial clusters |
| Dendritic spines |
Synaptic plasticity, local protein synthesis |
Recruited during [LTP[/entities/[long-term-potentiation[/entities/[long-term-potentiation[/entities/[long-term-potentiation[/entities/[long-term-potentiation--TEMP--/entities)--FIX--; [mTOR[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration--TEMP--/mechanisms)--FIX---regulated |
| Growth cones |
Cytoskeletal remodeling during axon guidance |
Highly dynamic; fission/fusion rapid |
The balance between fission and fusion determines mitochondrial size and mobility:
- Fission generates small, mobile mitochondria transported by kinesin (anterograde) and dynein (retrograde) motors along microtubules
- Fusion generates large, interconnected networks that share matrix contents, complementing damaged components
- Syntaphilin anchors mitochondria at synapses, creating stationary pools at active zones
Calcium signals from synaptic activity regulate mitochondrial dynamics:
- Low-moderate Ca[2]⁺: Activates CaMKII → [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- Ser616 phosphorylation → moderate fission for mitochondrial redistribution
- High Ca[2]⁺: Activates calcineurin → [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- Ser637 dephosphorylation → excessive fission; simultaneously triggers OMA1-mediated OPA1 cleavage (inhibiting fusion)
- Excitotoxic Ca[2]⁺ (e.g., [NMDA receptor[/entities/[nmda-receptor[/entities/[nmda-receptor[/entities/[nmda-receptor[/entities/[nmda-receptor--TEMP--/entities)--FIX-- receptor]] receptor overactivation): Triggers massive [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- recruitment, mitochondrial fragmentation, cytochrome c release, and apoptosis
Synaptic activity dynamically modulates mitochondrial dynamics:
- Neuronal activity promotes fission near synapses, generating small mitochondria for transport to active zones
- Prolonged quiescence favors fusion, creating large interconnected networks in the soma
- [BDNF[/proteins/[bdnf[/proteins/[bdnf[/proteins/[bdnf[/proteins/[bdnf--TEMP--/proteins)--FIX-- signaling (via TrkB → ERK → [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- Ser616) promotes mitochondrial fission and redistribution to synapses supporting plasticity
AD features the most comprehensively documented mitochondrial dynamics disruption:
- Excessive fragmentation: Reduced MFN1/2 and OPA1 expression combined with increased [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- levels and activity shift the balance toward fission (Wang et al., 2009)
- [Amyloid-Beta[/proteins/[Amyloid-Beta[/proteins/[Amyloid-Beta[/proteins/[Amyloid-Beta[/proteins/[Amyloid-Beta[/proteins//proteins/[Amyloid-Beta--TEMP--/proteins/)--FIX-- effects: [Aβ[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta--TEMP--/entities)--FIX-- oligomers directly interact with [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX--, enhancing its GTPase activity; [Aβ[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta--TEMP--/entities)--FIX-- also reduces MFN2 expression and disrupts ER-mitochondria tethering
- [Tau[/entities/[tau-protein[/entities/[tau-protein[/entities/[tau-protein[/entities/[tau-protein--TEMP--/entities)--FIX--(/proteins/tau pathology: Hyperphosphorylated tau] impairs mitochondrial transport along axons by destabilizing microtubule tracks; tau] also aberrantly interacts with DRP1
- Impaired transport: Kinesin-mediated anterograde transport of mitochondria to synapses is reduced in AD [neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons--TEMP--/entities)--FIX--, leading to synaptic energy deficit
- Consequences: Fragmented, dysfunctional mitochondria produce less ATP, generate more [reactive oxygen species[/mechanisms/[oxidative-stress[/mechanisms/[oxidative-stress[/mechanisms/[oxidative-stress[/mechanisms/[oxidative-stress--TEMP--/mechanisms)--FIX--, buffer calcium poorly, and fail to support synaptic transmission — contributing directly to [synaptic dysfunction[/mechanisms/[synaptic-dysfunction[/mechanisms/[synaptic-dysfunction[/mechanisms/[synaptic-dysfunction[/mechanisms/[synaptic-dysfunction--TEMP--/mechanisms)--FIX-- and cognitive decline
PD is the disease most directly linked to mitochondrial dynamics through [genetics[/mechanisms/[genetics[/mechanisms/[genetics[/mechanisms/[genetics[/mechanisms/[genetics--TEMP--/mechanisms)--FIX--:
- [PINK1[/proteins/[parkin[/proteins/[parkin[/proteins/[parkin[/proteins/[parkin--TEMP--/proteins)--FIX-- mitophagy pathway: [PINK1[/proteins/[pink1-protein[/proteins/[pink1-protein[/proteins/[pink1-protein[/proteins/[pink1-protein--TEMP--/proteins)--FIX-- accumulates on depolarized mitochondria, recruits Parkin (E3 ubiquitin ligase), which ubiquitinates outer membrane proteins (MFN1/2, VDAC, Miro) to trigger mitophagy. This pathway requires upstream [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX---mediated fission to generate mitochondria small enough for autophagosomal engulfment
- MFN2 as Parkin substrate: Parkin ubiquitinates MFN2, targeting it for degradation; this prevents fusion of damaged mitochondria with healthy ones
- [LRRK2[/proteins/[alpha-synuclein[/proteins/[alpha-synuclein[/proteins/[alpha-synuclein[/proteins/[alpha-synuclein--TEMP--/proteins)--FIX-- toxicity: Overexpression of α-synuclein fragments mitochondria in a [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX---dependent manner and inhibits SNARE-mediated ER-mitochondria contacts
- Selective vulnerability: [Dopaminergic neurons[/cell-types/[dopaminergic-neurons-snpc[/cell-types/[dopaminergic-neurons-snpc[/cell-types/[dopaminergic-neurons-snpc[/cell-types/[dopaminergic-neurons-snpc--TEMP--/cell-types)--FIX-- of the [substantia nigra[/brain-regions/[substantia-nigra[/brain-regions/[substantia-nigra[/brain-regions/[substantia-nigra[/brain-regions/[substantia-nigra--TEMP--/brain-regions)--FIX-- have exceptionally long, highly branched axons with enormous bioenergetic demands, making them particularly sensitive to mitochondrial dynamics disruption
- Mutant [huntingtin[/proteins/[huntingtin[/proteins/[huntingtin[/proteins/[huntingtin[/proteins/[huntingtin--TEMP--/proteins)--FIX-- directly binds [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX--, stimulating its enzymatic activity and causing excessive mitochondrial fragmentation in [medium spiny neurons[/cell-types/[medium-spiny-neurons[/cell-types/[medium-spiny-neurons[/cell-types/[medium-spiny-neurons[/cell-types/[medium-spiny-neurons--TEMP--/cell-types)--FIX-- (Song et al., 2011)
- Reduced MFN1 and OPA1 levels in HD [striatum[/brain-regions/[striatum[/brain-regions/[striatum[/brain-regions/[striatum[/brain-regions/[striatum--TEMP--/brain-regions)--FIX--
- Impaired mitochondrial transport in corticostriatal axons due to mHTT interference with motor protein complexes
- Mitochondrial calcium handling defects in [MSNs[/cell-types/[motor-neurons[/cell-types/[motor-neurons[/cell-types/[motor-neurons[/cell-types/[motor-neurons--TEMP--/cell-types)--FIX-- are among the longest cells in the body; mitochondrial transport defects are an early pathological feature in ALS
- Mutant [SOD1[/proteins/[tdp-43[/proteins/[tdp-43[/proteins/[tdp-43[/proteins/[tdp-43--TEMP--/proteins)--FIX-- and [FUS[/proteins/[fus-protein[/proteins/[fus-protein[/proteins/[fus-protein[/proteins/[fus-protein--TEMP--/proteins)--FIX-- pathology affects mitochondrial dynamics through multiple mechanisms
- [C9orf72[/genes/[c9orf72[/genes/[c9orf72[/genes/[c9orf72[/genes/[c9orf72--TEMP--/genes)--FIX-- dipeptide repeat proteins impair mitochondrial function and dynamics
| Gene |
Disease |
Mechanism |
| MFN2 |
Charcot-Marie-Tooth type 2A |
Impaired outer membrane fusion; disrupted ER-mito tethering |
| OPA1 |
Autosomal dominant optic atrophy (ADOA) |
Impaired inner membrane fusion; cristae remodeling defects |
| DNM1L (DRP1) |
Lethal encephalopathy; epileptic encephalopathy |
Impaired mitochondrial (and peroxisomal) fission |
| MFF |
Encephalopathy with optic atrophy |
Impaired [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- recruitment to mitochondria |
| GDAP1 |
CMT types 4A and 2K |
Impaired mitochondrial fission in peripheral nerves |
| Approach |
Compound |
Mechanism |
Status |
| [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- GTPase inhibitor |
Mdivi-1 |
Originally described as [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- inhibitor; now recognized to have significant off-target effects (Complex I inhibition) |
Research tool; too non-specific for clinical use |
| [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX---FIS1 interaction blocker |
P110 peptide |
Selectively blocks pathological (stress-induced) fission while preserving physiological fission |
Preclinical; brain-penetrant; efficacy in AD, PD, HD, ALS, TBI models |
| Novel [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- inhibitors |
SC9, others |
Structure-based design targeting [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- GTPase domain |
Early discovery |
- MFN2 agonists: Small molecules promoting mitofusin conformational activation are being developed for CMT2A and potentially broader neurodegeneration applications
- OPA1 stabilizers: Compounds that prevent OMA1-mediated cleavage of L-OPA1, preserving inner membrane fusion capacity
- Gene therapy: AAV-mediated delivery of MFN2 or OPA1 to affected [neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons--TEMP--/entities)--FIX--
Enhancing the removal of fragmented, damaged mitochondria:
- [PINK1[/proteins/[parkin[/proteins/[parkin[/proteins/[parkin[/proteins/[parkin--TEMP--/proteins)--FIX-- pathway activators (USP30 inhibitors, PINK1 stabilizers)
- [mTOR[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration--TEMP--/mechanisms)--FIX-- inhibition (rapamycin) to enhance autophagy/mitophagy
- NAD⁺ precursors (NR, NMN) to boost mitochondrial biogenesis and SIRT1/3-mediated quality control
- Urolithin A (mitophagy inducer; in [clinical trials[/[clinical-trials[/[clinical-trials[/[clinical-trials[/[clinical-trials[/[clinical-trials[/[clinical-trials[/[clinical-trials[/clinical-trials for aging-related conditions)
Given that neurodegeneration involves disruption of the entire dynamics-transport-quality control axis:
- Fission reduction + fusion enhancement: Restoring the fission/fusion balance
- Dynamics modulation + bioenergetic support: CoQ10, MitoQ (mitochondria-targeted antioxidants)
- Dynamics modulation + transport rescue: Enhancing kinesin/dynein-mediated mitochondrial motility
- Dynamics modulation + mitophagy: Ensuring damaged fragments are cleared
The study of Mitochondrial Dynamics has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying [mechanisms of neurodegeneration[/[mechanisms[/[mechanisms[/[mechanisms[/[mechanisms[/[mechanisms[/[mechanisms[/[mechanisms[/mechanisms and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
- [/diseases/alzheimers[/diseases/[alzheimers[/diseases/[alzheimers[/diseases/[alzheimers[/diseases/[alzheimers--TEMP--/diseases)--FIX--
- [/mechanisms/amyloid-hypothesis[/mechanisms/[amyloid-hypothesis[/mechanisms/[amyloid-hypothesis[/mechanisms/[amyloid-hypothesis[/mechanisms/[amyloid-hypothesis--TEMP--/mechanisms)--FIX--
- [/mechanisms/tau-pathology[/mechanisms/[tau-pathology[/mechanisms/[tau-pathology[/mechanisms/[tau-pathology[/mechanisms/[tau-pathology--TEMP--/mechanisms)--FIX--
- [/diseases/parkinsons[/diseases/[parkinsons[/diseases/[parkinsons[/diseases/[parkinsons[/diseases/[parkinsons--TEMP--/diseases)--FIX--
- [/mechanisms/alpha-synuclein[/mechanisms/[alpha-synuclein[/mechanisms/[alpha-synuclein[/mechanisms/[alpha-synuclein[/mechanisms/[alpha-synuclein--TEMP--/mechanisms)--FIX--
- [Detmer SA & Chan DC. (2007. [Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol, 8:870-879.)(https://doi.org/10.1038/nrm2275)
- [Chen H & Chan DC. (2009. [Mitochondrial dynamics — fusion, fission, movement, and mitophagy — in neurodegenerative diseases. Hum Mol Genet, 18:R169-R176.)(https://doi.org/10.1093/hmg/ddp326)
- [Wang X, et al. (2009. [Impaired balance of mitochondrial fission and fusion in Alzheimer's Disease. J Neurosci, 29:9090-9103.)(https://doi.org/10.1523/JNEUROSCI.1357-09.2009)
- [Song W, et al. (2011. [Mutant huntingtin binds the mitochondrial fission GTPase DRP1 and increases its enzymatic activity. Nat Med, 17:377-382.)(https://doi.org/10.1038/nm.2453)
- [Friedman JR, et al. (2011. ER tubules mark sites of mitochondrial division. Science, 334:358-362.)
- [Bertholet AM, et al. (2016. Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity. Neurobiol Dis, 90:3-19.)
- [Borber V, et al. (2023. Mitochondrial dynamics in neurodegenerative diseases: unraveling the role of fusion and fission processes. Int J Mol Sci, 24:13033.)
- [Cho DH, et al. (2009. S-nitrosylation of DRP1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science, 324:102-105.)
- [Youle RJ & van der Bliek AM. (2012. Mitochondrial fission, fusion, and stress. Science, 337:1062-1065.)
- [Züchner S, et al. (2004. Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nat Genet, 36:449-451.)
- [Alexander C, et al. (2000. OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat Genet, 26:211-215.)
- [Liu W, et al. (2021. [Mitochondrial fusion and fission proteins in Parkinson's Disease. Ageing Res Rev, 67:101265.)](https://doi.org/10.1016/j.arr.2021.101265]## See Also)
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- [DRP1[/entities/[drp1[/entities/[drp1[/entities/[drp1[/entities/[drp1--TEMP--/entities)--FIX-- — Primary fission GTPase
-
- [PINK1[/genes/[pink1[/genes/[pink1[/genes/[pink1[/genes/[pink1--TEMP--/genes)--FIX--/proteins/parkin] — E3 ubiquitin ligase for mitophagy
-
- [autophagy[/entities/[autophagy[/entities/[autophagy[/entities/[autophagy[/entities/[autophagy--TEMP--/entities)--FIX-- — Clearance of damaged mitochondria
-
- [Alzheimer's disease[/diseases/[alzheimers[/diseases/[alzheimers[/diseases/[alzheimers[/diseases/[alzheimers--TEMP--/diseases)--FIX-- — Mitochondrial dysfunction in AD
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- [Parkinson's disease[/diseases/[parkinsons[/diseases/[parkinsons[/diseases/[parkinsons[/diseases/[parkinsons--TEMP--/diseases)--FIX-- — PINK1/Parkin mitophagy pathway
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- [Huntington's disease[/mechanisms/[huntington-pathway[/mechanisms/[huntington-pathway[/mechanisms/[huntington-pathway[/mechanisms/[huntington-pathway--TEMP--/mechanisms)--FIX-- — mHTT disrupts mitochondrial dynamics
-
- [ALS[/diseases/[als[/diseases/[als[/diseases/[als[/diseases/[als--TEMP--/diseases)--FIX-- — Motor neuron [mitochondrial dysfunction[/mechanisms/[mitochondrial-dysfunction[/mechanisms/[mitochondrial-dysfunction[/mechanisms/[mitochondrial-dysfunction[/mechanisms/[mitochondrial-dysfunction--TEMP--/mechanisms)--FIX--
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- [Entities Index/entities)