Autophagy and neurodegeneration
Open accessAbstract
Most neurodegenerative diseases that afflict humans are associated with the intracytoplasmic deposition of aggregate-prone proteins in neurons. Autophagy is a powerful process for removing such proteins. In this Review, we consider how certain neurodegenerative diseases may be associated with impaired autophagy and how this may affect pathology. We also discuss how autophagy induction may be a plausible therapeutic strategy for some conditions and review studies in various models that support this hypothesis. Finally, we briefly describe some of the signaling pathways that may be amenable to therapeutic targeting for these goals.
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Molecular and histopathologic analyses of patient tissues demonstrate mislocalized or accumulated autophagy machinery, pathogenic mutations underlying familial neurodegenerative diseases disable known autophagy-related factors, and genetically ablating autophagy effectors produces neurodegeneration in cell and animal model systems, supporting a role for autophagy dysfunction in age-related neurode
“Molecular and histopathologic analyses of patient tissues demonstrate mislocalized or accumulated autophagy machinery, pathogenic mutations underlying familial neurodegenerative diseases disable known autophagy-related factors, and genetically ablating autophagy effectors produce neurodegeneration in cell and animal model systems [74–81], supporting a role for autophagy dysfunction in the devel”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [76]
Autophagy proteins have been shown to impact the clearance of protein aggregates in neurons, most likely by canonical aggrephagy.
“While autophagy proteins have been shown to impact the clearance of protein aggregates in neurons, most likely by the canonical autophagic process of aggrephagy (Frake et al., 2015; Menzies et al., 2017; Qaisiya et al., 2017; Sarkar et al., 2007; Sarkar et al., 2009; Webb et al., 2003; Yamamoto and Simonsen, 2011), effects in microglia of the CNS are more likely due to LANDO.”
From LC3-Associated Endocytosis Facilitates β-Amyloid Clearance and Mitigates Neurodegeneration in Murine Alzheimer’s Disease (2019) · cites this paper as Frake et al., 2015
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Research works printed but not linked: 2
- Rubinsztein DC, Shpilka T, Elazar Z. Mecha- nisms of autophagosome biogenesis. Curr Biol. 2012;22(1):R29-R34.
- Rubinsztein DC. The roles of intracellular pro- tein-degradation pathways in neurodegenera- tion. Nature. 2006;443(7113):780-786.
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- Authors
- Frake, R. A., Ricketts, T., Menzies, F. M., & Rubinsztein, D. C.
- Corresponding author
- Rubinsztein, David C.
- Venue
- Journal of Clinical Investigation
- Published
- 2015-01-02
- Volume
- 125
- Issue
- 1
- Pages
- 65-74
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC4382230
- OpenAlex
- W2029582543
- Cited by
- 332
- References
- 153
- Citations by year
- 2026: 17 · 2025: 14 · 2024: 19 · 2023: 28 · 2022: 18 · 2021: 36 · 2020: 38 · 2019: 30 · 2018: 40 · 2017: 37 · 2016: 36 · 2015: 19
- FWCI
- 5.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Apollo (University of Cambridge) (submittedVersion)
- Funders
- Wellcome Trust (100140, 095317)
- National Institute for Health and Care Research
- Tau Consortium
- Medical Research Council
- Cambridge Institute for Medical Research, University of Cambridge
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- autophagy, neurodegenerative diseases, protein aggregation, protein clearance, autophagy dysfunction, therapeutic targeting, signaling pathways, neuronal pathology
- MeSH terms
- Animals, Autophagy, Humans, Neurodegenerative Diseases, Protein Kinase Inhibitors, TOR Serine-Threonine Kinases
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