Cited by 1,472Heat shock proteins researchGenetics, Aging, and Longevity in Model OrganismsUbiquitin and proteasome pathways

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The Biology of Proteostasis in Aging and Disease

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Labbadia, Johnathan, Morimoto, Richard I·2015·Annual Review of Biochemistry

DOI 10.1146/annurev-biochem-060614-033955PMC PMC4539002

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Abstract

Loss of protein homeostasis (proteostasis) is a common feature of aging and disease that is characterized by the appearance of nonnative protein aggregates in various tissues. Protein aggregation is routinely suppressed by the proteostasis network (PN), a collection of macromolecular machines that operate in diverse ways to maintain proteome integrity across subcellular compartments and between tissues to ensure a healthy life span. Here, we review the composition, function, and organizational properties of the PN in the context of individual cells and entire organisms and discuss the mechanisms by which disruption of the PN, and related stress response pathways, contributes to the initiation and progression of disease. We explore emerging evidence that disease susceptibility arises from early changes in the composition and activity of the PN and propose that a more complete understanding of the temporal and spatial properties of the PN will enhance our ability to develop effective treatments for protein conformational diseases.

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Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,897
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024

Show all 182 references

Research works printed but not linked: 1

Martinez-Vicente M, 2008, J. Clin. Investig., 118, 777

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Single-nucleus RNA sequencing demonstrates an autosomal dominant Alzheimer’s disease profile and possible mechanisms of disease protection
Almeida, M. C., Eger, S. J., He, C., Audouard, M., Nikitina, A. A., Glasauer, S. M. K., Han, D., Mejía‐Cupajita, B., Acosta‐Uribe, J., Villalba‐Moreno, N. D., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.02.009 · Cited by 34
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Intramembrane proteolysis within lysosomes
Schröder, B., & Säftig, P. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.012 · Cited by 28
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Daniele, S., Pietrobono, D., Fusi, J., Gerfo, A. L., Cerri, E., Chico, L., Iofrida, C., Petrozzi, L., Baldacci, F., Giacomelli, C., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00017 · Cited by 28
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Châari, A. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.02.148 · Cited by 27
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Papanagnou, E., Gumeni, S., Sklirou, A. D., Rafeletou, A., Terpos, E., Keklikoglou, K., Kastritis, E., Stamatelopoulos, K. S., Sykiotis, G. P., Dimopoulos, M. A., et al. (2022) · Aging Cell · doi:10.1111/acel.13715 · Cited by 32
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Lee, T., Chen, P., Su, M. P., Li, J., Chang, Y., Liu, R., Juan, H., Yang, J., Chan, S., Tsai, Y., et al. (2021) · Aging Cell · doi:10.1111/acel.13379 · Cited by 27
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Authors: Labbadia, J., & Morimoto, R. I.
Affiliations: Department of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University, Evanston, Illinois 60208;
Northwestern University (US)
Corresponding author: Morimoto, Richard I
ORCID: Morimoto, Richard I
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 2015-06-02
Volume: 84
Issue: 1
Pages: 435-464
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev-biochem-060614-033955
PMC: PMC4539002
OpenAlex: W2152231829
Cited by: 1,472
References: 182
Citations by year: 2026: 142 · 2025: 127 · 2024: 150 · 2023: 152 · 2022: 140 · 2021: 148 · 2020: 143 · 2019: 139 · 2018: 136 · 2017: 106 · 2016: 69 · 2015: 19
FWCI: 10.55
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Annual Review of Biochemistry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
UCL Discovery (University College London) (submittedVersion)
Funders: Ellison Medical Foundation
National Institutes of Health (5p50mh094267-05)
National Institute on Aging (R37AG026647, R01AG026647)
National Institute of Mental Health (P50-MH094267)
National Institute of General Medical Sciences (P50GM081892, R01GM038109, R37GM038109)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: proteostasis, proteostasis network, aging, protein aggregation, stress response pathways, protein conformational diseases, disease susceptibility, lifespan
MeSH terms: Aging, Animals, Humans, Proteins, Neurodegenerative Diseases, Metabolic Networks and Pathways, Proteolysis, Endoplasmic Reticulum Stress

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