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TAX1BP1 recruitment reactivates autophagy of Tau aggregates through ULK1 and TBK1

Bauer, B.; Schuschnig, M.; Martens, S.

2026-02-13 cell biology
10.64898/2026.02.12.705532 bioRxiv
Show abstract

The accumulation of protein aggregates is a hallmark of numerous neurodegenerative diseases. These aggregates frequently accumulate ubiquitin and the early autophagy factor p62 yet fail to undergo degradation. Whether such aggregates are principally susceptible to autophagic clearance is unknown. Here, we show that Tau aggregates associated with Alzheimers disease (AD) and other tauopathies persist due to defective autophagy initiation. This autophagy resistance correlates with a block in the recruitment of the autophagy receptor TAX1BP1 and the downstream machinery to the aggregates. Artificial targeting of TAX1BP1 to Tau aggregates restores their autophagic turnover. Mechanistically, TAX1BP1 co-activates ULK1- and TBK1-dependent signaling, thereby enabling aggregate sequestration by autophagosomes. We identify exclusion of the TAX1BP1 receptor as a breaking point at which pathological Tau aggregates evade autophagy. Furthermore, we show that Tau aggregates can be rendered susceptible to autophagy, revealing therapeutic strategies for their clearance in disease.

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