The proteasome: overview of structure and functions
Open accessAbstract
The proteasome is a highly sophisticated protease complex designed to carry out selective, efficient and processive hydrolysis of client proteins. It is known to collaborate with ubiquitin, which polymerizes to form a marker for regulated proteolysis in eukaryotic cells. The highly organized proteasome plays a prominent role in the control of a diverse array of basic cellular activities by rapidly and unidirectionally catalyzing biological reactions. Studies of the proteasome during the past quarter of a century have provided profound insights into its structure and functions, which has appreciably contributed to our understanding of cellular life. Many questions, however, remain to be elucidated.
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PSMC5 lacks a HbYX motif and does not directly open the 20S CP gated channel.
“Although PSMC5 lacks a HbYX motif and thus does not directly open the 20S CP gated channel [7, 38]”
From PSMC5 insufficiency and P320R mutation impair proteasome function (2024) · cites this paper as [7]
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β2 Subunit Propeptides Influence Cooperative Proteasome Assembly
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Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly
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Self-citationThe Axial Channel of the 20S Proteasome Opens Upon Binding of the PA200 Activator
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PI31 is a modulator of proteasome formation and antigen processing
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The Assembly Pathway of the 19S Regulatory Particle of the Yeast 26S Proteasome
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Natural Compounds with Proteasome Inhibitory Activity for Cancer Prevention and Treatment
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Chapter 3 Thymic Microenvironments for T-Cell Repertoire Formation
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Inhibition of Ubiquitin-mediated Proteolysis by the Arabidopsis 26 S Protease Subunit S5a
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UBL/UBA Ubiquitin Receptor Proteins Bind a Common Tetraubiquitin Chain
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Novel Propeptide Function in 20 S Proteasome Assembly Influences β Subunit Composition
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Rad23 and Rpn10: perennial wallflowers join the m�l�e
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Molecular Basis for Proline- and Arginine-Rich Peptide Inhibition of Proteasome
Anbanandam, A., Albarado, D. C., Tı̂rziu, D., Simons, M., & Veeraraghavan, S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.021 · Cited by 62 · see citing works
Blm10 binds to pre‐activated proteasome core particles with open gate conformation
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PACemakers of Proteasome Core Particle Assembly
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Proteasomes from structure to function: perspectives from Archaea.
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REGγ proteasome activator is involved in the maintenance of chromosomal stability
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Nucleotide excision repair and the ubiquitin proteasome pathway—Do all roads lead to Rome?
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Self-citationChaperone-driven proteasome assembly
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Modest cortex and promiscuous medulla for thymic repertoire formation
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Self-citationProteasome gene duplications in mammals, flies and plants.
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Reactive Oxygen Species in Metabolic and Inflammatory Signaling
Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081 · see citing works
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 · see citing works
Targeting proteins for degradation.
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Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171 · see citing works
Santos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168 · see citing works
Kröll‐Hermi, A., Ebstein, F., Stoetzel, C., Geoffroy, V., Schaefer, E., Scheidecker, S., Bär, S., Takamiya, M., Kawakami, K., Zieba, B. A., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.201911861 · Cited by 65 · see citing works
Mechanisms of substrate recognition by the 26S proteasome
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ZFAND5/ZNF216 is an activator of the 26S proteasome that stimulates overall protein degradation
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The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?
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Ebstein, F., Küry, S., Most, V., Rosenfelt, C., Scott-Boyer, M.-P., van Woerden, G. M., Besnard, T., Papendorf, J. J., Studencka-Turski, M., Wang, T., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo3189 · Cited by 36 · see citing works
Understanding the mammalian TRAP complex function(s)
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Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy
Kitajima, Y., Suzuki, N., Yoshioka, K., Izumi, R., Tateyama, M., Tashiro, Y., Takahashi, R., Aoki, M., & Ono, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00859 · Cited by 14 · see citing works
“The 26S proteasome is composed of one barrel-shaped proteolytic core complex (20S proteasome), capped at both ends with 19S regulatory complexes, which recognize ubiquitinated proteins (Baumeister et al., 1998; Tanaka, 2009).”
BackgroundDeb, W., Rosenfelt, C., Vignard, V., Papendorf, J. J., Möller, S., Wendlandt, M., Studencka-Turski, M., Cogné, B., Besnard, T., Ruffier, L., et al. (2024) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2024.05.016 · Cited by 11 · see citing works
Küry, S., Stanton, J. E., van Woerden, G., Hsieh, T.-C., Rosenfelt, C., Scott-Boyer, M. P., Most, V., Wang, T., Papendorf, J. J., de Konink, C., et al. (2024) · doi:10.1101/2024.01.13.24301174 · Cited by 6 · see citing works
PSMC5 insufficiency and P320R mutation impair proteasome function
Yu, Z.-Q., Carmichael, J., Collins, G. A., D'Agostino, M. D., Lessard, M., Firth, H. V., Harijan, P., Fry, A. E., Dean, J., Zhang, J., et al. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae085 · Cited by 4 · see citing works
“Typically, the 19S RP binds to one or both ends of the 20S CP to form proteasome holoenzymes, which are accordingly termed single-capped 26S proteasomes and double-capped 30S proteasomes [4, 7].”
Küry, S., Stanton, J. E., van Woerden, G. M., Bosc-Rosati, A., Hsieh, T.-C., Bray, L., Oloudé, M., Rosenfelt, C., Scott-Boyer, M. P., Most, V., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65556-8 · Cited by 3 · see citing works
“2a and Supplementary Table 2) and underlines previous fi ndings in mice and plants 23,24 .”
- Authors
- TANAKA, K.
- Affiliations
- Tokyo Metropolitan Institute of Medical Science (JP)
- Corresponding author
- TANAKA, Keiji
- ORCID
- TANAKA, Keiji
- Venue
- Proceedings of the Japan Academy, Series B
- Publisher
- Japan Academy
- Published
- 2009
- Volume
- 85
- Issue
- 1
- Pages
- 12-36
- ISSN
- 0386-2208 (ISSN-L)
- 1349-2896
- PMC
- PMC3524306
- OpenAlex
- W2070367241
- Cited by
- 862
- References
- 143
- Citations by year
- 2026: 55 · 2025: 80 · 2024: 69 · 2023: 90 · 2022: 95 · 2021: 95 · 2020: 84 · 2019: 63 · 2018: 38 · 2017: 26 · 2016: 12 · 2015: 17 · 2014: 30 · 2013: 28 · 2012: 21
- FWCI
- 1.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the Japan Academy Series B (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- proteasome, proteasome structure, proteasome function, ubiquitin, ubiquitin-proteasome system, regulated proteolysis, protein degradation, protease complex
- MeSH terms
- Endopeptidases, Molecular Chaperones, Ubiquitin, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex
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