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Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
Open accessAbstract
Alzheimer's amyloid precursor protein 695 (APP) is a plasma membrane protein, which is known to be the source of the toxic amyloid beta (Abeta) peptide associated with the pathogenesis of Alzheimer's disease (AD). Here we demonstrate that by virtue of its chimeric NH2-terminal signal, APP is also targeted to mitochondria of cortical neuronal cells and select regions of the brain of a transgenic mouse model for AD. The positively charged residues at 40, 44, and 51 of APP are critical components of the mitochondrial-targeting signal. Chemical cross-linking together with immunoelectron microscopy show that the mitochondrial APP exists in NH2-terminal inside transmembrane orientation and in contact with mitochondrial translocase proteins. Mutational studies show that the acidic domain, which spans sequence 220-290 of APP, causes the transmembrane arrest with the COOH-terminal 73-kD portion of the protein facing the cytoplasmic side. Accumulation of full-length APP in the mitochondrial compartment in a transmembrane-arrested form, but not lacking the acidic domain, caused mitochondrial dysfunction and impaired energy metabolism. These results show, for the first time, that APP is targeted to neuronal mitochondria under some physiological and pathological conditions.
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“We generated a mutant APP that does not localize to the mitochondria by deleting the mitochondrial targeting domain (residues 40–51) (42). We then compared the protection against mitophagy in Jurkat cells expressing either WT-APP or the mutant (Mut)-APP, which showed decreased localization to the mitochondria of the Jurkat cells than the WT-APP (Figure 3G, H).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [42]
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“accumulating data certainly do suggest APP and Aβ, as well as the entire γ-secretase complex, physically associate with mitochondria and can effect changes in mitochondrial function [58-67].”
From The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives (2014) · cites this paper as [61]
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Metadata
- Authors
- Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G.
- Affiliations
- University of Pennsylvania (US)
- ORCID
- Avadhani, Narayan G.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2003-04-14
- Volume
- 161
- Issue
- 1
- Pages
- 41-54
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2172865
- OpenAlex
- W2132988134
- Cited by
- 571
- References
- 47
- Citations by year
- 2026: 11 · 2025: 12 · 2024: 18 · 2023: 22 · 2022: 16 · 2021: 24 · 2020: 23 · 2019: 18 · 2018: 35 · 2017: 14 · 2016: 27 · 2015: 24 · 2014: 17 · 2013: 24 · 2012: 31
- FWCI
- 13.60
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1r01gm034483-01a3)
- National Institute of General Medical Sciences (GM34483)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- amyloid precursor protein, APP695, mitochondrial targeting, mitochondrial dysfunction, energy metabolism, Alzheimer's disease, amyloid-beta, mitochondrial translocase, acidic domain, cortical neurons, transgenic mouse model, crosslinking, immunoelectron microscopy
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Brain, Cell Compartmentation, Cells, Cultured, Disease Models, Animal, Energy Metabolism, Humans, Immunohistochemistry, Intracellular Membranes, Mice, Transgenic, Microscopy, Electron, Mitochondria, Molecular Conformation, Neurons, Recombinant Fusion Proteins, Amyloid beta-Protein Precursor, Protein Structure, Tertiary, Protein Transport, Cytochrome-c Oxidase Deficiency, Mice
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