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Updated: Aug 5, 2026

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
Targeting Ubiquitinated Protein Aggregates in Neurodegenerative Diseases: current Status and Future Directions
Masahiko Takahashi1, Takayuki Abe1, Masahiro Fujii1
1Division of Virology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Molecular and Cellular Biology
|August 4, 2026
Summary
Cellular stress triggers stress granules (SGs), which can become toxic aggregates in neurodegenerative diseases like ALS and Alzheimer's. Targeting pathways regulating SG dynamics, such as USP10, may offer therapeutic benefits.
Area of Science:
- Neurobiology
- Cellular Biology
- Molecular Medicine
Background:
- Cellular stressors induce stress granules (SGs), dynamic RNA-protein complexes.
- Dysregulated SG dynamics can lead to persistent, pathological protein inclusions.
- SG conversion into aggregates is implicated in neurodegenerative diseases like ALS and Alzheimer's.
Purpose of the Study:
- To review molecular factors regulating SG assembly and disassembly.
- To explore pathological processes converting SGs into neurotoxic aggregates.
- To highlight the role of USP10 in SG dynamics and neurodegeneration.
Main Methods:
- Literature review of recent advances in SG research.
- Analysis of molecular mechanisms underlying SG formation and resolution.
- Examination of the role of specific proteins, including USP10, in disease pathogenesis.
Main Results:
- SGs are transient under normal stress but can form persistent inclusions.
- TDP-43 and Tau pathology in SGs contribute to neurotoxicity in ALS and AD.
- USP10 modulates SG dynamics and is mechanistically linked to ALS and AD.
Conclusions:
- Targeting SG assembly/disassembly pathways is a potential therapeutic strategy.
- Understanding SG conversion to aggregates is crucial for neurodegenerative disease treatment.
- USP10 presents a promising target for mitigating neurodegenerative disease progression.
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