ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013
Synaptic protein α1-takusan mitigates amyloid-β-induced synaptic loss via interaction with tau and postsynaptic density-95 at postsynaptic sites.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 19 citations in OpenAlex.
- Transcriptome and Translatome Regulation of Pathogenesis in Alzheimer's Disease Model Mice.Journal of Alzheimer's disease : JAD · 2022Article
- The role of pathological tau in synaptic dysfunction in Alzheimer's diseases.Translational neurodegeneration · 2021Review
- Alzheimer's Disease: An Overview of Major Hypotheses and Therapeutic Options in Nanotechnology.Nanomaterials (Basel, Switzerland) · 2020Review
- NitroSynapsin therapy for a mouse MEF2C haploinsufficiency model of human autism.Nature communications · 2017Article
- Roles of tau protein in health and disease.Acta neuropathologica · 2017Review
- Multiple faces of dynamin-related protein 1 and its role in Alzheimer's disease pathogenesis.Biochimica et biophysica acta · 2016Review
- RPS23RG1 reduces Aβ oligomer-induced synaptic and cognitive deficits.Scientific reports · 2016Article
- Oligomeric Aβ-induced synaptic dysfunction in Alzheimer's disease.Molecular neurodegeneration · 2014Review
- Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease.Biochemical pharmacology · 2014Review
- Soluble beta-amyloid peptides, but not insoluble fibrils, have specific effect on neuronal microRNA expression.PloS one · 2014Article
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11 authors at 1 institution in 1 country.
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Abstract
The synaptic toxicity of soluble amyloid-β (Aβ) oligomers plays a critical role in the pathophysiology of Alzheimer's disease (AD). Here we report that overexpressed α1-takusan, which we previously identified as a protein that enhances synaptic activity via interaction with PSD-95, mitigates oligomeric Aβ-induced synaptic loss. In contrast, takusan knockdown results in enhanced synaptic damage. α1-Takusan interacts with tau either directly or indirectly, and prevents Aβ-induced tau hyperphosphorylation and mitochondrial fragmentation. Deletion analysis identified the second domain (D2) within the takusan protein that is required for PSD-95 clustering and synaptic protection from Aβ. A 51 aa sequence linking D2 to the PDZ-binding C terminus was found to be as effective as full-length takusan in protecting synapses from Aβ-induced damage. Moreover, a sequence containing the D2 from the human protein discs large homolog 5, when linked to a C-terminal PDZ-binding motif, can also increase the clustering of PSD-95 in cortical dendrites. In summary, α1-takusan protects synapses from Aβ-induced insult via interaction with PSD-95 and tau. Thus, takusan-based protein sequences from either mouse or human may be of potential therapeutic benefit in AD.
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