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Distinct autophagy impairment mechanisms of huntingtin aggregates with different polyQ lengths
Different ways huntingtin protein clumps with varying polyQ lengths disrupt cell cleanup
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Abstract
PolyQ length-dependent mechanisms reveal that polyQ103 aggregates evade autophagy recognition.
- PolyQ aggregates in Huntington's disease vary in length, affecting how they impair autophagy.
- PolyQ103 aggregates avoid recognition by the autophagy receptor SQSTM1/p62.
- PolyQ43 condensates are recognized by SQSTM1/p62, but their size prevents full autophagosome formation.
- Overexpressing optineurin preferentially binds to polyQ103 aggregates, enhancing cell survival.
- K63-ubiquitination on polyQ103 aggregates is crucial for recruiting optineurin.
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