Frontotemporal dementia (FTD) accounts for approximately 10% of neurodegenerative disease cases where proteins aggregate into amyloid filaments.
Researchers at the Medical Research Council (MRC) Laboratory of Molecular Biology in Cambridge, UK, have used cryo-electron microscopy (cryo-EM) to identify the protein TAF15 as the culprit in this type of FTD.
FTD involves the degeneration of the frontal and temporal lobes of the brain, impacting emotions, personality, behavior, speech, and word comprehension.
It is typically diagnosed in people aged 45 to 65. While FUS was previously suspected of aggregating in this type of FTD, cryo-EM revealed that the protein aggregates had the same atomic structure in multiple brains, and it was identified as TAF15.
Understanding the molecular basis of this form of FTD opens doors to developing diagnostic tests and therapies similar to strategies for Alzheimer’s disease.
Cryo-EM plays a crucial role in advancing our understanding of neurodegenerative diseases by providing insights into protein structures beyond the capabilities of previous technologies.
Moreover, some individuals with FTD also have motor neuron disease, and this study identified the same aggregated structure of TAF15 in brain regions associated with motor neuron disease. This finding suggests TAF15 may contribute to both conditions, warranting further research.
Understanding the protein structures underlying these diseases is essential for developing diagnostic tools and therapies.
The next steps involve screening for abnormal protein aggregates in more patient samples to assess their prevalence.
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The research findings can be found in Nature.
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