DOI: 10.1073/pnas.1120559109. Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach

Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach

10.1073/pnas.1120559109

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

The 26S proteasome is at the executive end of the ubiquitin-proteasome pathway for the controlled degradation of intracellular proteins. While the structure of its 20S core particle (CP) has been determined by X-ray crystallography, the structure of the 19S regulatory particle (RP), which recruits substrates, unfolds them, and translocates them to the CP for degradation, has remained elusive. Here, we describe the molecular architecture of the 26S holocomplex determined by an integrative approach based on data from cryoelectron microscopy, X-ray crystallography, residue-specific chemical cross-linking, and several proteomics techniques. The “lid” of the RP (consisting of Rpn3/5/6/7/8/9/11/12) is organized in a modular fashion. Rpn3/5/6/7/9/12 form a horseshoe-shaped heterohexamer, which connects to the CP and roofs the AAA-ATPase module, positioning the Rpn8/Rpn11 heterodimer close to its mouth. Rpn2 is rigid, supporting the lid, while Rpn1 is conformationally variable, positioned at the periphery of the ATPase ring. The ubiquitin receptors Rpn10 and Rpn13 are located in the distal part of the RP, indicating that they were recruited to the complex late in its evolution. The modular structure of the 26S proteasome provides insights into the sequence of events prior to the degradation of ubiquitylated substrates.

Bibliography

Lasker, K., FÃ¶rster, F., Bohn, S., Walzthoeni, T., Villa, E., Unverdorben, P., Beck, F., Aebersold, R., Sali, A., & Baumeister, W. (2012). Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proceedings of the National Academy of Sciences, 109(5), 1380â1387.

Authors 10

Keren Lasker (first)
Friedrich Förster (additional)
Stefan Bohn (additional)
Thomas Walzthoeni (additional)
Elizabeth Villa (additional)
Pia Unverdorben (additional)
Florian Beck (additional)
Ruedi Aebersold (additional)
Andrej Sali (additional)
Wolfgang Baumeister (additional)

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Dates

Type	When
Created	13 years, 6 months ago (Jan. 24, 2012, 2:18 a.m.)
Deposited	3 years, 2 months ago (June 7, 2022, 5:17 a.m.)
Indexed	2 weeks, 4 days ago (Aug. 3, 2025, 12:15 a.m.)
Issued	13 years, 6 months ago (Jan. 23, 2012)
Published	13 years, 6 months ago (Jan. 23, 2012)
Published Online	13 years, 6 months ago (Jan. 23, 2012)
Published Print	13 years, 6 months ago (Jan. 31, 2012)

Funders 0

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BibTeX

@article{Lasker_2012, title={Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach}, volume={109}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.1120559109}, DOI={10.1073/pnas.1120559109}, number={5}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Lasker, Keren and Förster, Friedrich and Bohn, Stefan and Walzthoeni, Thomas and Villa, Elizabeth and Unverdorben, Pia and Beck, Florian and Aebersold, Ruedi and Sali, Andrej and Baumeister, Wolfgang}, year={2012}, month=jan, pages={1380–1387} }

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  "abstract": "<jats:p>The 26S proteasome is at the executive end of the ubiquitin-proteasome pathway for the controlled degradation of intracellular proteins. While the structure of its 20S core particle (CP) has been determined by X-ray crystallography, the structure of the 19S regulatory particle (RP), which recruits substrates, unfolds them, and translocates them to the CP for degradation, has remained elusive. Here, we describe the molecular architecture of the 26S holocomplex determined by an integrative approach based on data from cryoelectron microscopy, X-ray crystallography, residue-specific chemical cross-linking, and several proteomics techniques. The \u201clid\u201d of the RP (consisting of Rpn3/5/6/7/8/9/11/12) is organized in a modular fashion. Rpn3/5/6/7/9/12 form a horseshoe-shaped heterohexamer, which connects to the CP and roofs the AAA-ATPase module, positioning the Rpn8/Rpn11 heterodimer close to its mouth. Rpn2 is rigid, supporting the lid, while Rpn1 is conformationally variable, positioned at the periphery of the ATPase ring. The ubiquitin receptors Rpn10 and Rpn13 are located in the distal part of the RP, indicating that they were recruited to the complex late in its evolution. The modular structure of the 26S proteasome provides insights into the sequence of events prior to the degradation of ubiquitylated substrates.</jats:p>",
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