Cited by 435Autophagy in Disease and TherapyAlzheimer's disease research and treatmentsCalcium signaling and nucleotide metabolism

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Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases

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Nixon, Ralph A., Rubinsztein, David C.·2024·Nature Reviews Molecular Cell Biology

DOI 10.1038/s41580-024-00757-5PMC PMC12239022

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Abstract

Autophagy is a lysosome-based degradative process used to recycle obsolete cellular constituents and eliminate damaged organelles and aggregate-prone proteins. Their postmitotic nature and extremely polarized morphologies make neurons particularly vulnerable to disruptions caused by autophagy-lysosomal defects, especially as the brain ages. Consequently, mutations in genes regulating autophagy and lysosomal functions cause a wide range of neurodegenerative diseases. Here, we review the role of autophagy and lysosomes in neurodegenerative diseases such as Alzheimer disease, Parkinson disease and frontotemporal dementia. We also consider the strong impact of cellular ageing on lysosomes and autophagy as a tipping point for the late-age emergence of related neurodegenerative disorders. Many of these diseases have primary defects in autophagy, for example affecting autophagosome formation, and in lysosomal functions, especially pH regulation and calcium homeostasis. We have aimed to provide an integrative framework for understanding the central importance of autophagic-lysosomal function in neuronal health and disease.

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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
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Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214
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
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365
Self-citation
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
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Show all 319 references

Research works printed but not linked: 3

Lees, M. B. Basic Neurochemistry 5th edn, Vol. 39 (Raven Press, 1994).
de Duve, C. Lysosomes, a New Group of Cytoplasmic Particle (Ronald Press, 1959).
Chou, C. C. et al. Proteostasis and lysosomal quality control deficits in Alzheimer’s disease neurons. Preprint at bioRxiv https://doi.org/10.1101/2023.03.27.534444 (2023). · DOI

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Authors: Nixon, R. A., & Rubinsztein, D. C.
Affiliations: Nathan Kline Institute for Psychiatric Research (US)
University of Cambridge (GB)
Corresponding author: Nixon, Ralph A.
ORCID: Nixon, Ralph A.
Rubinsztein, David C.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2024-08-06
Volume: 25
Issue: 11
Pages: 926-946
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/s41580-024-00757-5
PMC: PMC12239022
OpenAlex: W4401363901
Cited by: 435
References: 319
Citations by year: 2026: 260 · 2025: 160 · 2024: 14
FWCI: 26.31
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by
www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion, cc-by)
Apollo (University of Cambridge) (submittedVersion, cc-by)
Apollo (cc-by)
Funders: CHDI Foundation
Rainwater Charitable Foundation
Alzheimer's Society
National Institute for Health and Care Research ((NIHR203312)
Department of Health and Social Care
Parkinson's UK
Rosetrees Trust
UK Dementia Research Institute
Medical Research Council (NIHR203312)
NIHR Cambridge Biomedical Research Centre (NIHR 203312)
National Institute on Aging (P01AG017617, R01AG062376)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: autophagy, lysosomes, neurodegenerative diseases, Alzheimer's disease, Parkinson's disease, frontotemporal dementia, neuronal aging, autophagosome formation, calcium homeostasis, protein aggregate clearance, lysosomal storage disease
MeSH terms: Autophagosomes, Animals, Autophagy, Humans, Lysosomes, Neurons, Neurodegenerative Diseases

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Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases

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