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A prion-like domain of TFEB mediates the co-aggregation of TFEB and mHTT

Autophagy. 2022-06; 
Junsheng Yang, Huilin Xu, Chaoyue Zhang, Xiaotong Yang, Weijie Cai, Xiaoli Chen
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摘要

The aggregation of mutant HTT (huntingtin; mHTT) is a hallmark of Huntington disease (HD). mHTT aggregates interact and sequester dozens of proteins and affect diverse key cellular functions. Here we report that TFEB (transcription factor EB), a master regulator of lysosome biogenesis and autophagy, is yet another protein that co-aggregates with mHTT. We also found the mHTT-TFEB co-aggregation is mediated by a prion-like domain (PrLD) near the N terminus of TFEB. Our findings point out a possible limitation for therapeutic strategies targeting TFEB to clear mHTT, and also provided a possible explanation for controversies that TFEB overexpression lowered soluble mHTT in some HD models but failed to reduce mHTT a... More

关键词

Aggregate, HD, TFEB, mHTT, prion-like domain