DOI: 10.1073/pnas.1510449112. Structural characterization of the interaction of Ubp6 with the 26S proteasome

Structural characterization of the interaction of Ubp6 with the 26S proteasome

10.1073/pnas.1510449112

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Significance In eukaryotic cells the 26S proteasome is responsible for the regulated degradation of intracellular proteins. The function of this large macromolecular machine is regulated by many cofactors, most notably the deubiquitylating enzyme ubiquitin C-terminal hydrolase 6 (Ubp6). Here, we investigate the structure of Ubp6 bound to the 26S proteasome and explore its influence on the conformational landscape of the 26S proteasome. Our structure reveals that Ubp6’s active site may contribute to a large composite active site, also formed by the mouth of the proteasomal ATPase ring and the active site of deubiquitylating enzyme regulatory particle non-ATPase 11. Moreover, Ubp6 modulates the conformational landscape of the proteasome, favoring an intermediate state, which may explain the effects of Ubp6 on proteasomal degradation.

Bibliography

Aufderheide, A., Beck, F., Stengel, F., Hartwig, M., Schweitzer, A., Pfeifer, G., Goldberg, A. L., Sakata, E., Baumeister, W., & FÃ¶rster, F. (2015). Structural characterization of the interaction of Ubp6 with the 26S proteasome. Proceedings of the National Academy of Sciences, 112(28), 8626â8631.

Authors 10

Antje Aufderheide (first)
Florian Beck (additional)
Florian Stengel (additional)
Michaela Hartwig (additional)
Andreas Schweitzer (additional)
Günter Pfeifer (additional)
Alfred L. Goldberg (additional)
Eri Sakata (additional)
Wolfgang Baumeister (additional)
Friedrich Förster (additional)

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Dates

Type	When
Created	10 years, 1 month ago (July 1, 2015, 12:42 a.m.)
Deposited	3 years, 2 months ago (June 7, 2022, 8:52 a.m.)
Indexed	2 weeks, 5 days ago (Aug. 2, 2025, 12:55 a.m.)
Issued	10 years, 1 month ago (June 30, 2015)
Published	10 years, 1 month ago (June 30, 2015)
Published Online	10 years, 1 month ago (June 30, 2015)
Published Print	10 years, 1 month ago (July 14, 2015)

Funders 3

Ludwig-Maximilians-Universität München 10.13039/501100005722
Region: Europe
gov (Local government)
Labels3
1. Ludwig Maximilians University Munich
2. LMU Munich
3. LMU
Awards1
1. CIPSM
Deutsche Forschungsgemeinschaft 10.13039/501100001659
Region: Europe
gov (National government)
Labels3
1. German Research Association
2. German Research Foundation
3. DFG
Awards1
1. SFB-1035
Deutsche Forschungsgemeinschaft 10.13039/501100001659
Region: Europe
gov (National government)
Labels3
1. German Research Association
2. German Research Foundation
3. DFG
Awards1
1. SFB-969

BibTeX

@article{Aufderheide_2015, title={Structural characterization of the interaction of Ubp6 with the 26S proteasome}, volume={112}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.1510449112}, DOI={10.1073/pnas.1510449112}, number={28}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Aufderheide, Antje and Beck, Florian and Stengel, Florian and Hartwig, Michaela and Schweitzer, Andreas and Pfeifer, Günter and Goldberg, Alfred L. and Sakata, Eri and Baumeister, Wolfgang and Förster, Friedrich}, year={2015}, month=jun, pages={8626–8631} }

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