PIAS1 regulates mutant Huntingtin accumulation and Huntington’s disease-associated phenotypes in vivo
Open accessAbstract
The disruption of protein quality control networks is central to pathology in Huntington's disease (HD) and other neurodegenerative disorders. The aberrant accumulation of insoluble high-molecular-weight protein complexes containing the Huntingtin (HTT) protein and SUMOylated protein corresponds to disease manifestation. We previously identified an HTT-selective E3 SUMO ligase, PIAS1, that regulates HTT accumulation and SUMO modification in cells. Here we investigated whether PIAS1 modulation in neurons alters HD-associated phenotypes in vivo. Instrastriatal injection of a PIAS1-directed miRNA significantly improved behavioral phenotypes in rapidly progressing mutant HTT (mHTT) fragment R6/2 mice. PIAS1 reduction prevented the accumulation of mHTT and SUMO- and ubiquitin-modified proteins, increased synaptophysin levels, and normalized key inflammatory markers. In contrast, PIAS1 overexpression exacerbated mHTT-associated phenotypes and aberrant protein accumulation. These results confirm the association between aberrant accumulation of expanded polyglutamine-dependent insoluble protein species and pathogenesis, and they link phenotypic benefit to reduction of these species through PIAS1 modulation.
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Mutant huntingtin accumulates in many cell types and in multiple forms, due at least in part to failure of protein quality control networks, as reflected by accumulation of ubiquitin and other post-translationally-modified proteins and disruptions in autophagy.
“Pathologically, mHTT accumulates in many cells types, and in multiple forms, due at least in part to the failure of protein quality control networks, as reflected by an accumulation of ubiquitin and other post-translationally-modified proteins (Ochaba et al. , 2016) and disruptions in autophagy (Kurosawa et al. , 2015).”
From Microglial depletion prevents extracellular matrix changes and striatal volume reduction in a model of Huntington's disease (2020) · cites this paper as Ochaba et al., 2016
Protein clearance by ubiquitin and autophagy is severely impaired in Huntington's disease, shown by accumulated ubiquitinated species in patient and mouse brain and increased p62.
“Ubiquitinand autophagy-based protein clearance systems are highly impaired in Huntington's disease, as evidenced by a striking build-up of ubiquitinated species in patient brain and mouse models”
From Microglial depletion prevents extracellular matrix changes and striatal volume reduction in a model of Huntington's disease (2020) · cites this paper as Ochaba et al., 2016
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- Authors
- Ochaba, J., Monteys, A. M., O’Rourke, J. G., Reidling, J. C., Steffan, J. S., Davidson, B. L., & Thompson, L. M.
- Affiliations
- University of California, Irvine (US)
- Children's Hospital of Philadelphia (US)
- Cedars-Sinai Medical Center (US)
- Corresponding author
- Thompson, Leslie M.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2016-05
- Volume
- 90
- Issue
- 3
- Pages
- 507-520
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4942306
- OpenAlex
- W2337933333
- Cited by
- 94
- References
- 72
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 11 · 2023: 8 · 2022: 14 · 2021: 10 · 2020: 8 · 2019: 12 · 2018: 12 · 2017: 10
- FWCI
- 6.38
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (P30CA062203)
- National Institute of Neurological Disorders and Stroke (R56NS072453, R01NS052789, R01NS090390, R56NS090390, R01NS076631, R01NS072453)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Health Sciences › Medicine › Physiology › Lysosomal Storage Disorders Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- PIAS1, Huntington's disease, mutant huntingtin, SUMOylation, SUMO E3 ligase, protein quality control, polyglutamine expansion, protein aggregation, R6/2 mice, microRNA, synaptophysin, neuroinflammation, ubiquitination, neurodegeneration
- MeSH terms
- Huntingtin Protein, Animals, Brain, Disease Models, Animal, Humans, Huntington Disease, Mutation, Nerve Tissue Proteins, Neurons, Nuclear Proteins, Phenotype, Small Ubiquitin-Related Modifier Proteins, Protein Inhibitors of Activated STAT, Mice
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