Nature Communications (Feb 2022)
Allosteric control of Ubp6 and the proteasome via a bidirectional switch
- 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
Affiliations
- Ka Ying Sharon Hung
- Department of Cell Biology, Harvard Medical School
- Sven Klumpe
- Department of Molecular Structural Biology, Max Planck Institute of Biochemistry
- Markus R. Eisele
- Department of Molecular Structural Biology, Max Planck Institute of Biochemistry
- Suzanne Elsasser
- Department of Cell Biology, Harvard Medical School
- Geng Tian
- Department of Cell Biology, Harvard Medical School
- Shuangwu Sun
- Department of Cell Biology, Harvard Medical School
- Jamie A. Moroco
- Department of Chemistry and Chemical Biology, Northeastern University
- Tat Cheung Cheng
- Department of Molecular Structural Biology, Max Planck Institute of Biochemistry
- Tapan Joshi
- Department of Molecular Structural Biology, Max Planck Institute of Biochemistry
- Timo Seibel
- Department of Cell Biology, Harvard Medical School
- Duco Van Dalen
- Leiden University Medical Center
- Xin-Hua Feng
- Life Sciences Institute (LSI), Zhejiang University
- Ying Lu
- Department of Systems Biology, Harvard Medical School
- Huib Ovaa
- Leiden University Medical Center
- John R. Engen
- Department of Chemistry and Chemical Biology, Northeastern University
- Byung-Hoon Lee
- Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology (DGIST)
- Till Rudack
- Biospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum
- Eri Sakata
- Department of Molecular Structural Biology, Max Planck Institute of Biochemistry
- Daniel Finley
- Department of Cell Biology, Harvard Medical School
- DOI
- https://doi.org/10.1038/s41467-022-28186-y
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 13
Abstract
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.
