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Aggregation and propagation of TAF15 trigger neurodegeneration
Lanxia Meng1, Congcong Liu1, Huangchuan Gong1
1Department of Neurology, Renmin Hospital of Wuhan University, Wuhan 430060, China.
Neuron
|August 6, 2026
Summary
TATA-binding protein-associated factor 15 (TAF15) forms self-propagating amyloid fibrils. These fibrils cause neurodegeneration and cognitive deficits in mice, indicating TAF15 aggregation drives disease.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Protein misfolding and aggregation are implicated in neurodegenerative diseases.
- Frontotemporal lobar degeneration (FTLD) involves amyloid fibril formation.
- The role of TATA-binding protein-associated factor 15 (TAF15) in neurodegeneration is unclear.
Purpose of the Study:
- To investigate if TAF15 amyloid fibrils propagate in a prion-like manner.
- To determine if TAF15 aggregation drives neurodegeneration.
Main Methods:
- Induction of TAF15 amyloid fibril formation in vitro.
- Stereotactic injection of synthetic TAF15 fibrils into wild-type mouse brains.
- Assessment of endogenous TAF15 aggregation and pathology.
- Behavioral testing (cognitive, anxiety, depression) in mice.
- Genetic deletion of endogenous TAF15 to assess protective effects.
Main Results:
- Synthetic TAF15 fibrils were shown to self-propagate.
- Injection of TAF15 fibrils induced aggregation of endogenous TAF15 and cell-to-cell transmission.
- TAF15 pathology led to cortical neuron degeneration, cognitive impairment, and behavioral deficits.
- Genetic deletion of TAF15 abolished the detrimental effects of TAF15 fibrils.
Conclusions:
- TAF15 amyloid fibrils can self-propagate and induce neurodegeneration.
- TAF15 aggregation is a causative factor in neurodegenerative processes.
- TAF15 represents a potential therapeutic target for related neurodegenerative diseases.
