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: | , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-28186-y |
| _version_ | 1818977024655491072 |
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| author | 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 |
| author_facet | 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 |
| author_sort | Ka Ying Sharon Hung |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-20T16:21:10Z |
| format | Article |
| id | doaj.art-0db17aeb4b8c4a309992d0d564111f7b |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T16:21:10Z |
| publishDate | 2022-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-0db17aeb4b8c4a309992d0d564111f7b2022-12-21T19:33:36ZengNature PortfolioNature Communications2041-17232022-02-0113111310.1038/s41467-022-28186-yAllosteric control of Ubp6 and the proteasome via a bidirectional switchKa Ying Sharon Hung0Sven Klumpe1Markus R. Eisele2Suzanne Elsasser3Geng Tian4Shuangwu Sun5Jamie A. Moroco6Tat Cheung Cheng7Tapan Joshi8Timo Seibel9Duco Van Dalen10Xin-Hua Feng11Ying Lu12Huib Ovaa13John R. Engen14Byung-Hoon Lee15Till Rudack16Eri Sakata17Daniel Finley18Department of Cell Biology, Harvard Medical SchoolDepartment of Molecular Structural Biology, Max Planck Institute of BiochemistryDepartment of Molecular Structural Biology, Max Planck Institute of BiochemistryDepartment of Cell Biology, Harvard Medical SchoolDepartment of Cell Biology, Harvard Medical SchoolDepartment of Cell Biology, Harvard Medical SchoolDepartment of Chemistry and Chemical Biology, Northeastern UniversityDepartment of Molecular Structural Biology, Max Planck Institute of BiochemistryDepartment of Molecular Structural Biology, Max Planck Institute of BiochemistryDepartment of Cell Biology, Harvard Medical SchoolLeiden University Medical CenterLife Sciences Institute (LSI), Zhejiang UniversityDepartment of Systems Biology, Harvard Medical SchoolLeiden University Medical CenterDepartment of Chemistry and Chemical Biology, Northeastern UniversityDepartment of New Biology, Daegu Gyeongbuk Institute of Science and Technology (DGIST)Biospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University BochumDepartment of Molecular Structural Biology, Max Planck Institute of BiochemistryDepartment of Cell Biology, Harvard Medical SchoolThe 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.https://doi.org/10.1038/s41467-022-28186-y |
| spellingShingle | 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 Allosteric control of Ubp6 and the proteasome via a bidirectional switch Nature Communications |
| title | Allosteric control of Ubp6 and the proteasome via a bidirectional switch |
| title_full | Allosteric control of Ubp6 and the proteasome via a bidirectional switch |
| title_fullStr | Allosteric control of Ubp6 and the proteasome via a bidirectional switch |
| title_full_unstemmed | Allosteric control of Ubp6 and the proteasome via a bidirectional switch |
| title_short | Allosteric control of Ubp6 and the proteasome via a bidirectional switch |
| title_sort | allosteric control of ubp6 and the proteasome via a bidirectional switch |
| url | https://doi.org/10.1038/s41467-022-28186-y |
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