The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
Open accessAbstract
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.
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Citations
Cites
Integrative structure modeling of macromolecular assemblies from proteomics data
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Self-citation
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Molecular architecture of the yeast Mediator complex
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“In a few studies, structural biologists have developed complete bioinformatic workflows providing 3D hybrid models of macromolecular protein complexes at different levels of detail (17,28).”
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Faini, M., Stengel, F., & Aebersold, R. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1382-4 · Cited by 44
Self-citationGenetic interaction mapping informs integrative structure determination of protein complexes
Braberg, H., Echeverria, I., Bohn, S., Cimermancic, P., Shiver, A., Alexander, R., Xu, J., Shales, M., Dronamraju, R., Jiang, S., et al. (2020) · Science · doi:10.1126/science.aaz4910 · Cited by 37
Self-citationMolecular Mechanisms of Bortezomib Action: Novel Evidence for the miRNA–mRNA Interaction Involvement
Łuczkowska, K., Rogińska, D., Ulańczyk, Z., Paczkowska, E., Schmidt, C. A., & Machaliński, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21010350 · Cited by 26
CyToStruct: augmenting the network visualization of cytoscape with the power of molecular viewers
Nepomnyachiy, S., Ben-Tal, N., & Kolodny, R. (2015) · Structure · doi:10.1016/j.str.2015.02.013 · Cited by 20
Developments in integrative modeling with dynamical interfaces
Ozdemir, E. S., Nussinov, R., Gursoy, A., & Keskin, O. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.10.007 · Cited by 17
Metadata
- Authors
- Lasker, K., Förster, F., Bohn, S., Walzthoeni, T., Villa, E., Unverdorben, P., Beck, F., Aebersold, R., Sali, A., & Baumeister, W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2012-01-23
- Volume
- 109
- Issue
- 5
- Pages
- 1380-1387
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2046164706
- Cited by
- 442
- References
- 1
- FWCI
- 25.21
- Type
- journal article
- Language
- en
- Open access
- green
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