The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Genetic Evidence Linking Age-Dependent Attenuation of the 26S Proteasome with the Aging Process
Open accessAbstract
The intracellular accumulation of unfolded or misfolded proteins is believed to contribute to aging and age-related neurodegenerative diseases. However, the links between age-dependent proteotoxicity and cellular protein degradation systems remain poorly understood. Here, we show that 26S proteasome activity and abundance attenuate with age, which is associated with the impaired assembly of the 26S proteasome with the 19S regulatory particle (RP) and the 20S proteasome. In a genetic gain-of-function screen, we characterized Rpn11, which encodes a subunit of the 19S RP, as a suppressor of expanded polyglutamine-induced progressive neurodegeneration. Rpn11 overexpression suppressed the age-related reduction of the 26S proteasome activity, resulting in the extension of flies' life spans with suppression of the age-dependent accumulation of ubiquitinated proteins. On the other hand, the loss of function of Rpn11 caused an early onset of reduced 26S proteasome activity and a premature age-dependent accumulation of ubiquitinated proteins. It also caused a shorter life span and an enhanced neurodegenerative phenotype. Our results suggest that maintaining the 26S proteasome with age could extend the life span and suppress the age-related progression of neurodegenerative diseases.
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Cites
Autophagy fights disease through cellular self-digestion
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Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
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Self-citationImpairment of the Ubiquitin-Proteasome System by Protein Aggregation
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Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome
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Regulation of Mammalian Autophagy in Physiology and Pathophysiology
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The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899
The proteasome: overview of structure and functions
TANAKA, K. (2009) · Proceedings of the Japan Academy, Series B · doi:10.2183/pjab.85.12 · Cited by 862
Self-citationEnhancement of proteasome activity by a small-molecule inhibitor of USP14
Lee, B.-H., Lee, M. J., Park, S., Oh, D.-C., Elsasser, S., Chen, P.-C., Gartner, C., Dimova, N., Hanna, J., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 893
Metadata
- Authors
- Tonoki, A., Kuranaga, E., Tomioka, T., Hamazaki, J., Murata, S., Tanaka, K., & Miura, M.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2009-02-01
- Volume
- 29
- Issue
- 4
- Pages
- 1095-1106
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2164687214
- Cited by
- 288
- References
- 43
- FWCI
- 3.28
- Type
- journal article
- Language
- en
- Open access
- green
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- Tonoki, A., Kuranaga, E., Tomioka, T., Hamazaki, J., Murata, S., Tanaka, K., & Miura, M. (2009). Genetic Evidence Linking Age-Dependent Attenuation of the 26S Proteasome with the Aging Process. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.01227-08
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