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UXT chaperone prevents proteotoxicity by acting as an autophagy adaptor for p62-dependent aggrephagy

Nat Commun. 2021-03; 
Min Ji Yoon, Boyoon Choi, Eun Jin Kim, Jiyeon Ohk, Chansik Yang, Yeon-Gil Choi, Jinyoung Lee, Chanhee Kang, Hyun Kyu Song, Yoon Ki Kim, Jae-Sung Woo, Yongcheol Cho, Eui-Ju Choi, Hosung Jung, Chungho Kim
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Monoclonal Antibody Services HA-Xenopus p62 was purchased from GenScript Get A Quote

摘要

p62/SQSTM1 is known to act as a key mediator in the selective autophagy of protein aggregates, or aggrephagy, by steering ubiquitinated protein aggregates towards the autophagy pathway. Here, we use a yeast two-hybrid screen to identify the prefoldin-like chaperone UXT as an interacting protein of p62. We show that UXT can bind to protein aggregates as well as the LB domain of p62, and, possibly by forming an oligomer, increase p62 clustering for its efficient targeting to protein aggregates, thereby promoting the formation of the p62 body and clearance of its cargo via autophagy. We also find that ectopic expression of human UXT delays SOD1(A4V)-induced degeneration of motor neurons in a Xenopus model system, ... More

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