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Caspase-2 is a condensate-mediated deubiquitinase in protein quality control

Nature Cell Biology. 2024-10; 
Yingwei Ge , Lijie Zhou, Yesheng Fu , Lijuan He, Yi Chen , Dingchang Li , Yuping Xie , Jun Yang , Haitao Wu, Hongmiao Dai , Zhiqiang Peng , Yong Zhang , Shaoqiong Yi , Bo Wu 1, Xin Zhang, Yangjun Zhang , Wantao Ying 1, Chun-Ping Cui , Cui Hua Liu , Lingqiang Zhang
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Abstract

Protein ubiquitination plays a critical role in protein quality control in response to cellular stress. The excessive accumulation of ubiquitinated conjugates can be detrimental to cells and is recognized as a hallmark of multiple neurodegenerative diseases. However, an in-depth understanding of how the excessive ubiquitin chains are removed to maintain ubiquitin homeostasis post stress remains largely unclear. Here we found that caspase-2 (CASP2) accumulates in a ubiquitin and proteasome-positive biomolecular condensate, which we named ubstressome, following stress and functions as a deubiquitinase to remove overloaded ubiquitin chains on proteins prone to misfolding. Mechanistically, CASP2 binds to the poly-u... More

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