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Gel-like inclusions of C-terminal fragments of TDP-43 sequester and inhibit proteasomes in neurons

Riemenschneider, H.; Guo, Q.; Bader, J.; Frottin, F.; Farny, D.; Kleinberger, G.; Haass, C.; Mann, M.; Hartl, F. U.; Baumeister, W.; Hipp, M. S.; Meissner, F.; Fernandez-Busnadiego, R.; Edbauer, D.

2021-03-16 neuroscience
10.1101/2021.03.15.435268 bioRxiv
Show abstract

TDP-43 inclusions enriched in C-terminal fragments of ~25kDa ("TDP-25") are associated with neurodegeneration in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Here, we analyzed gain-of-function mechanisms of TDP-25 combining cryo-electron tomography, proteomics and functional assays. TDP-25 inclusions are amorphous with gel-like biophysical properties and sequester proteasomes adopting exclusively substrate-processing conformations. This leads to proteostasis impairment, further enhanced by pathogenic mutations. These findings bolster the importance of proteasome dysfunction in ALS/FTD.

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