Impaired GAPDH‐induced mitophagy contributes to the pathology of Huntington's disease
Open accessAbstract
Mitochondrial dysfunction is implicated in multiple neurodegenerative diseases. In order to maintain a healthy population of functional mitochondria in cells, defective mitochondria must be properly eliminated by lysosomal machinery in a process referred to as mitophagy. Here, we uncover a new molecular mechanism underlying mitophagy driven by glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) under the pathological condition of Huntington's disease (HD) caused by expansion of polyglutamine repeats. Expression of expanded polyglutamine tracts catalytically inactivates GAPDH (iGAPDH), which triggers its selective association with damaged mitochondria in several cell culture models of HD. Through this mechanism, iGAPDH serves as a signaling molecule to induce direct engulfment of damaged mitochondria into lysosomes (micro‐mitophagy). However, abnormal interaction of mitochondrial GAPDH with long polyglutamine tracts stalled GAPDH‐mediated mitophagy, leading to accumulation of damaged mitochondria, and increased cell death. We further demonstrated that overexpression of inactive GAPDH rescues this blunted process and enhances mitochondrial function and cell survival, indicating a role for GAPDH‐driven mitophagy in the pathology of HD.
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Expanded polyglutamine repeats of mutant huntingtin protein associate with GAPDH, potentially disrupting GAPDH-mediated trafficking of damaged mitochondria into the lysosomal system.
“The expanded polyglutamine repeats of mutant huntingtin protein have been shown to associate with GAPDH, potentially disrupting GAPDH-mediated trafficking of damaged mitochondria into the lysosomal system31.”
From GAPDH controls extracellular vesicle biogenesis and enhances the therapeutic potential of EV mediated siRNA delivery to the brain (2021) · cites this paper as [31]
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“…fragmentation (Cui et al, 2006; Reddy et al, 2011) and altering a process of mitophagy (Martin et al, 2015) (Fig 7) along with impairing mitochondrial trafficking and Ca2+ buffering capacity (Choo et al, 2004; Chang et al, 2006; Orr et al, 2008), collectively contribute to the pathology of HD.”
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- Authors
- Hwang, S., Disatnik, M., & Mochly‐Rosen, D.
- Affiliations
- Stanford Medicine (US)
- Corresponding author
- Mochly‐Rosen, Daria
- Venue
- EMBO Molecular Medicine
- Published
- 2015-08-12
- Volume
- 7
- Issue
- 10
- Pages
- 1307-1326
- ISSN
- 1757-4676 (ISSN-L)
- 1757-4684
- PMC
- PMC4604685
- OpenAlex
- W2130120481
- Cited by
- 153
- References
- 8
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 19 · 2023: 19 · 2022: 11 · 2021: 26 · 2020: 15 · 2019: 9 · 2018: 13 · 2017: 12 · 2016: 15
- FWCI
- 6.22
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- EMBO Molecular Medicine (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- University of Cambridge
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- Huntington's disease, mitophagy, glyceraldehyde-3-phosphate dehydrogenase, polyglutamine expansion, mitochondrial dysfunction, cell death, neurodegeneration
- MeSH terms
- Huntingtin Protein, Animals, Cell Survival, Humans, Huntington Disease, Mitochondria, Nerve Tissue Proteins, Nuclear Proteins, Polyglutamic Acid, PC12 Cells, Mice, Knockout, Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+), Mice, Rats, Mitophagy
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