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Bernd Bauer

@berndbauer.bsky.social

255 followers 302 following 11 posts

PhD Student in Sascha Martens Lab @MaxPerutzLabs studying how cells remove protein aggregates using autophagy.

Bernd Bauer @berndbauer.bsky.social · 14/02/2026

7/ In summary, Tau aggregates evade autophagy by excluding TAX1BP1, and forced recruitment of TAX1BP1 reactivates their degradation. TAX1BP1 assembles the upstream autophagy machinery via its SKICH domain to form an initiation hub that triggers autophagosome biogenesis.

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Bernd Bauer @berndbauer.bsky.social · 14/02/2026

6/ And this hub matters: Tethering individual components alone is not enough to induce autophagy (A). Only simultaneous recruitment of the upstream machinery promotes autophagy initiation(B).

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Bernd Bauer @berndbauer.bsky.social · 14/02/2026

5/ Mechanistically, TAX1BP1 recruits the upstream autophagy machinery, including the ULK1 complex and TBK1 (A), to assemble an initiation hub via its SKICH domain (B).

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Bernd Bauer @berndbauer.bsky.social · 14/02/2026

4/ If we bypass this blockade by artificially tethering TAX1BP1 to Tau aggregates (A), this is sufficient to trigger autophagic flux (B). → Aggregates are sequestered into autophagosomes (C) → And efficiently cleared (D)

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Bernd Bauer @berndbauer.bsky.social · 14/02/2026

3/ Why? These Tau aggregates fail to initiate autophagy. They exclude key upstream autophagy factors, most importantly the receptor TAX1BP1 (A+B) This mirrors our previous in vitro reconstitution work using post-mortem Tau fibrils.

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Bernd Bauer @berndbauer.bsky.social · 14/02/2026

2/ Using a reconstituted cellular system, we found that Tau aggregates, despite being ubiquitinated and recognized by the early autophagy receptor p62 (A), are not degraded by autophagy (B). This behaviour is consistent with what is seen in disease.

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