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.
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 |
Similar Items
-
The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle.
by: Sakata, E, et al.
Published: (2011) -
Highlighting the Proteasome: Using Fluorescence to Visualize Proteasome Activity and Distribution
by: Jin Gan, et al.
Published: (2019-03-01) -
Deubiquitination of BES1 by UBP12/UBP13 promotes brassinosteroid signaling and plant growth
by: Su-Hyun Park, et al.
Published: (2022-09-01) -
UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2
by: Hannes Vanhaeren, et al.
Published: (2020-03-01) -
The degradation-promoting roles of deubiquitinases Ubp6 and Ubp3 in cytosolic and ER protein quality control.
by: Hongyi Wu, et al.
Published: (2020-01-01)