Praja1 <scp>E3</scp> ubiquitin ligase and the role it plays in neurodegeneration
Protein aggregation and transmission are hallmarks of neurodegenerative diseases. Praja1 E3 ubiquitin ligase has been shown to suppress the aggregation of causative proteins in amyotrophic lateral sclerosis, frontotemporal lobar degeneration, Parkinson's disease, Huntington's disease, and spinocerebellar degeneration, which include transactivation response DNA-binding protein of 43 kDa, fused in sarcoma, superoxide dismutase 1, α-synuclein, huntingtin, and ataxin-3. Aoki et al. demonstrated that Praja1 ubiquitinates and degrades tau, a key molecule in tauopathies such as Alzheimer's disease, Pick's disease, progressive supranuclear palsy, and corticobasal syndrome, furthering our understanding of the role of Praja1 in neurodegenerative diseases and potential therapeutic approaches.
Authors
- Kazuhiko Watabe (ORCID: https://orcid.org/0000-0002-0245-3834)
Institutions
- Aichi Medical University (JP)
- Tokyo Metropolitan Institute of Medical Science (JP)
Publication Details
- Journal
- FEBS Journal
- Published
- 2025-12-30
- DOI
- https://doi.org/10.1111/febs.70383
- Primary Topic
- Amyotrophic Lateral Sclerosis Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00