Allosteric control of Ubp6 and the proteasome via a bidirectional switch

Allosteric control of Ubp6 and the proteasome via a bidirectional switch

The interplay of the proteasome and deubiquitinase Ubp6 is crucial for the degradation of ubiquitylated substrates. Here, the authors provide structural insights into the allosteric mechanism by which the activities of both Ubp6 and the proteasome are regulated.

Bibliographic Details
Main Authors: Ka Ying Sharon Hung, Sven Klumpe, Markus R. Eisele, Suzanne Elsasser, Geng Tian, Shuangwu Sun, Jamie A. Moroco, Tat Cheung Cheng, Tapan Joshi, Timo Seibel, Duco Van Dalen, Xin-Hua Feng, Ying Lu, Huib Ovaa, John R. Engen, Byung-Hoon Lee, Till Rudack, Eri Sakata, Daniel Finley
Format: Article
Language:English
Published: Nature Portfolio 2022-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-28186-y

Internet

https://doi.org/10.1038/s41467-022-28186-y

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