The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Proteasome Structure and Assembly
Open accessAbstract
The eukaryotic 26S proteasome is a large multi-subunit complex that degrades the majority of proteins in the cell under normal conditions. The 26S proteasome can be divided into two subcomplexes: the 19S regulatory particle (RP) and the 20S core particle (CP). Most substrates are first covalently modified by ubiquitin, which then directs them to the proteasome. The function of the RP is to recognize, unfold, deubiquitylate and translocate substrates into the CP, which contains the proteolytic sites of the proteasome. Given the abundance and subunit complexity of the proteasome, the assembly of this ~2.5 MDa complex must be carefully orchestrated to ensure its correct formation. In recent years, significant advances have been made in the understanding of proteasome assembly, structure and function. Technical advances in cryo-electron microscopy have resulted in a series of atomic cryo-EM structures of both human and yeast 26S proteasomes. These structures have illuminated new intricacies and dynamics of the proteasome. In this review, we focus on the mechanisms of proteasome assembly, particularly in light of recent structural information.
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Cites
Complete subunit architecture of the proteasome regulatory particle
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Molecular Architecture and Assembly of the Eukaryotic Proteasome
Tomko, R. J., & Hochstrasser, M. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060410-150257 · Cited by 376
Self-citationAcetylation-Mediated Proteasomal Degradation of Core Histones during DNA Repair and Spermatogenesis
Qian, M.-X., Pang, Y., Liu, C. H., Haratake, K., Du, B.-Y., Ji, D.-Y., Wang, G.-F., Zhu, Q.-Q., Song, W., Yu, Y., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.032 · Cited by 330
PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria
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Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts
Kapeta, S., Chondrogianni, N., & Gonos, E. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031575 · Cited by 234
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Mitochondrial metabolism promotes adaptation to proteotoxic stress
Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645
N-degron and C-degron pathways of protein degradation
Varshavsky, A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1816596116 · Cited by 544
Regulation of proteasome assembly and activity in health and disease
Rousseau, A., & Bertolotti, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0040-z · Cited by 510
Advances in targeted degradation of endogenous proteins
Röth, S., Fulcher, L. J., & Sapkota, G. P. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03112-6 · Cited by 92
Vimer, S., Ben-Nissan, G., Morgenstern, D., Kumar-Deshmukh, F., Polkinghorn, C., Quintyn, R. S., Vasil’ev, Y. V., Beckman, J. S., Elad, N., Wysocki, V. H., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00080 · Cited by 63
Metadata
- Authors
- Budenholzer, L., Cheng, C. L., Li, Y., & Hochstrasser, M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2017-11
- Volume
- 429
- Issue
- 22
- Pages
- 3500-3524
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2620578360
- Cited by
- 366
- References
- 7
- FWCI
- 11.74
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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