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Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
Open accessAbstract
The endosomal sorting complexes required for transport (ESCRTs) are required to sort integral membrane proteins into intralumenal vesicles of the multivesicular body (MVB). Mutations in the ESCRT-III subunit CHMP2B were recently associated with frontotemporal dementia and amyotrophic lateral sclerosis (ALS), neurodegenerative diseases characterized by abnormal ubiquitin-positive protein deposits in affected neurons. We show here that autophagic degradation is inhibited in cells depleted of ESCRT subunits and in cells expressing CHMP2B mutants, leading to accumulation of protein aggregates containing ubiquitinated proteins, p62 and Alfy. Moreover, we find that functional MVBs are required for clearance of TDP-43 (identified as the major ubiquitinated protein in ALS and frontotemporal lobar degeneration with ubiquitin deposits), and of expanded polyglutamine aggregates associated with Huntington's disease. Together, our data indicate that efficient autophagic degradation requires functional MVBs and provide a possible explanation to the observed neurodegenerative phenotype seen in patients with CHMP2B mutations.
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“CHMP2B downregulation or expression of disease-associated CHMP2B mutants in Drosophila and mammalian cell lines results in aberrant endosomal structures, impaired autophagosome maturation, and cytosolic TARDBP aggregates [264,265,268,269].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [268]
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“Further corroborating the central role of MVBs in the maintenance of neuronal proteostasis, MVBs are essential for the clearance of ubiquitinated TARDBP, which accumulates in ALS and frontotemporal lobar degeneration (Filimonenko et al, 2007).”
From Autophagy in major human diseases (2021) · cites this paper as Filimonenko et al, 2007
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Metadata
- Authors
- Filimonenko, M., Stuffers, S., Raiborg, C., Yamamoto, A., Malerød, L., Fisher, E. M. C., Isaacs, A., Brech, A., Stenmark, H., & Simonsen, A.
- Affiliations
- University of Oslo (NO)
- Columbia University (US)
- University College London (GB)
- MRC Prion Unit (GB)
- Corresponding author
- Simonsen, Anne
- ORCID
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2007-11-05
- Volume
- 179
- Issue
- 3
- Pages
- 485-500
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2064794
- OpenAlex
- W2103275390
- Cited by
- 626
- References
- 62
- Citations by year
- 2026: 13 · 2025: 26 · 2024: 20 · 2023: 15 · 2022: 18 · 2021: 35 · 2020: 29 · 2019: 27 · 2018: 41 · 2017: 31 · 2016: 46 · 2015: 34 · 2014: 43 · 2013: 36 · 2012: 40
- FWCI
- 29.80
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- multivesicular bodies, ESCRT, CHMP2B, autophagy, protein aggregates, neurodegenerative diseases, TDP-43, polyglutamine aggregates, Huntington's disease, amyotrophic lateral sclerosis, frontotemporal dementia, p62, ESCRT-III
- MeSH terms
- Autophagy, Cell Membrane, HeLa Cells, Humans, Huntington Disease, Models, Biological, Mutation, Nerve Tissue Proteins, Neurons, Phenotype, Protein Binding, Endosomes, Neurodegenerative Diseases, Ubiquitin, Endosomal Sorting Complexes Required for Transport
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