β-Amyloid Accumulation Impairs Multivesicular Body Sorting by Inhibiting the Ubiquitin-Proteasome System
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Increasing evidence links intraneuronal β-amyloid (Aβ 42 ) accumulation with the pathogenesis of Alzheimer’s disease (AD). In Aβ precursor protein (APP) mutant transgenic mice and in human AD brain, progressive intraneuronal accumulation of Aβ 42 occurs especially in multivesicular bodies (MVBs). We hypothesized that this impairs the MVB sorting pathway. We used the trafficking of the epidermal growth factor receptor (EGFR) and TrkB receptor to investigate the MVB sorting pathway in cultured neurons. We report that, during EGF stimulation, APP mutant neurons demonstrated impaired inactivation, degradation, and ubiquitination of EGFR. EGFR degradation is dependent on translocation from MVB outer to inner membranes, which is regulated by the ubiquitin-proteasome system (UPS). We provide evidence that Aβ accumulation in APP mutant neurons inhibits the activities of the proteasome and deubiquitinating enzymes. These data suggest a mechanism whereby Aβ accumulation in neurons impairs the MVB sorting pathway via the UPS in AD.
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In this model, Aβ accumulates along the endosomal/lysosomal pathway that leads to dysfunction of multivesicular bodies, causing impairment of the ubiquitin-proteasome system, which also controls the fate of NMDARs undergoing endocytic vesicular trafficking.
“In this model, Ab accumulates along the endosomal/lysomal pathway that leads to dysfunction of multivesicular bodies, causing impairment of the ubiquitin-proteasome system, 9 which also controls the fate of NMDARs undergoing endocytic vesicular trafficking.50”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [9]
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Experimental — accuracy not yet measuredThese cultures are characterized by progressive buildup of intraneuronal Aβ, which is derived from endogenous Aβ escaping exocytosis after cleavage of the APP SW mutant.
“These cultures are characterized by progressive buildup of intraneuronal Ab, which is derived from endogenous Ab escaping exocytosis after cleavage of the APP SW mutant.9,49”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [9]
The section on Aβ42 localization in cultured APP-mutant neurons reports intracellular Aβ42 staining in neurons carrying the Swedish APP mutation and describes staining for endogenous Aβ42. The Introduction describes APP cleavage as a possible route to Aβ production. Neither passage establishes progressive buildup in these cultures or that the retained Aβ escaped exocytosis. (LLM, conf=0.84)
Experimental — accuracy not yet measuredIntraneuronal Aβ buildup has been associated with disturbed protein trafficking and sorting.
“A number of studies have associated intraneuronal Ab buildup with hyperphosphorylation of tau protein, 8 disturbed protein trafficking and sorting, 9 reduced expression of synaptic proteins, 10 and mitochondrial dysfunction.11,12”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [9]
In one study, Aβ-induced abnormalities in MVB endocytic sorting were demonstrated in APP mutant neurons, which appeared to be due to impairment of the ubiquitin proteasome system (UPS).
“In one study, Aβ-induced abnormalities in MVB endocytic sorting were demonstrated in APP mutant neurons, which appeared to be due to impairment of the ubiquitin proteasome system (UPS; [2]).”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [2]
Abnormalities in MVB sorting are due to Aβ-dependent alterations in the ubiquitin-proteasome system.
“The study went on to provide evidence that abnormalities in MVB sorting were due to Aβ-dependent alterations in the ubiquitin-proteasome system (UPS).”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [2]
The MVB sorting pathway, not internalization or recycling, is altered in Aβ accumulating neurons.
“Using the well established endocytosis of the epidermal growth factor receptor (EGFR), this study demonstrated that specifically the MVB sorting pathway, and not internalization or the recycling pathway, was altered in Aβ accumulating neurons.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [2]
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- Authors
- Almeida, C. G., Takahashi, R. H., & Gouras, G. K.
- Affiliations
- Cornell University (US)
- Corresponding author
- Gouras, Gunnar K.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2006-04-19
- Volume
- 26
- Issue
- 16
- Pages
- 4277-4288
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6673997
- OpenAlex
- W2168538246
- Cited by
- 316
- References
- 59
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 11 · 2023: 26 · 2022: 18 · 2021: 12 · 2020: 17 · 2019: 20 · 2018: 14 · 2017: 15 · 2016: 14 · 2015: 15 · 2014: 10 · 2013: 20 · 2012: 18
- FWCI
- 11.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- Alzheimer's Association
- American Health Assistance Foundation
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01NS045677, NS 045677)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- amyloid-beta deposition, multivesicular bodies, ubiquitin-proteasome system, Alzheimer's disease, epidermal growth factor receptor, TrkB receptor, receptor degradation, ubiquitination, deubiquitinase, proteasome inhibition
- MeSH terms
- Animals, Cells, Cultured, Epidermal Growth Factor, Hippocampus, Humans, Male, Mice, Transgenic, Synaptic Vesicles, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Rats, Sprague-Dawley, Ubiquitin, Proteasome Endopeptidase Complex, Mice, Rats, Proteasome Inhibitors, ErbB Receptors
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