Cited by 174Alzheimer's disease research and treatmentsNeuroscience and Neuropharmacology ResearchNeuroinflammation and Neurodegeneration Mechanisms

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DAB1 and Reelin Effects on Amyloid Precursor Protein and ApoE Receptor 2 Trafficking and Processing

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Hoe, Hyang-Sook, Tran, Tracy S., Matsuoka, Yasuji, Howell, Brian W., Rebeck, G. William·2006·Journal of Biological Chemistry

DOI 10.1074/jbc.m602162200

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Abstract

Numerous cytoplasmic adaptor proteins, including JIP1, FE65, and X11alpha, affect amyloid precursor protein (APP) processing and Abeta production. Dab1 is another adaptor protein that interacts with APP as well as with members of the apoE receptor family. We examined the effect of Dab1 on APP and apoEr2 processing in transfected cells and primary neurons. Dab1 interacted with APP and apoEr2 and increased levels of their secreted extracellular domains and their cytoplasmic C-terminal fragments. These effects depended on the NPXY domains of APP and apoEr2 and on the phosphotyrosine binding domain of Dab1 but did not depend on phosphorylation of Dab1. Dab1 decreased the levels of APP beta-C-terminal fragment and secreted Abeta. Full-length Dab1 or its phosphotyrosine binding domain alone increased surface levels of APP, as determined by surface protein biotinylation and live cell staining. A ligand for apoEr2, the extracellular matrix protein Reelin, significantly increased the interaction of apoEr2 with Dab1. Surprisingly, we also found that Reelin treatment significantly increased the interaction of APP and Dab1. Moreover, Reelin treatment increased cleavage of APP and apoEr2 and decreased production of the beta-C-terminal fragment of APP and Abeta. Together, these data suggest that Dab1 alters trafficking and processing of APP and apoEr2, and this effect is influenced by extracellular ligands.

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Binding of F-spondin to amyloid-β precursor protein: a candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage
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Authors: Hoe, H.-S., Tran, T. S., Matsuoka, Y., Howell, B. W., & Rebeck, G. W.
Affiliations: Georgetown University Medical Center (US)
National Institutes of Health (US)
Corresponding author: Rebeck, G. William
ORCID: Tran, Tracy S.
Howell, Brian W.
Rebeck, G. William
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2006-11
Volume: 281
Issue: 46
Pages: 35176-35185
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m602162200
OpenAlex: W2058881577
Cited by: 174
References: 34
Citations by year: 2026: 4 · 2025: 6 · 2024: 7 · 2023: 7 · 2022: 5 · 2021: 5 · 2020: 3 · 2019: 1 · 2018: 6 · 2017: 9 · 2016: 13 · 2015: 8 · 2014: 12 · 2013: 14 · 2012: 12
FWCI: 9.13
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5084 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institute on Aging (R01AG014473, K01AG022455)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Dab1, reelin, amyloid precursor protein, APP processing, amyloid-beta, adaptor proteins, NPXY motif, phosphotyrosine binding domain, protein trafficking, extracellular matrix ligands, neurons
MeSH terms: Reelin Protein, Animals, Cell Line, Chlorocebus aethiops, Gene Expression Regulation, Humans, Nerve Tissue Proteins, Phosphorylation, Serine Endopeptidases, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, Amyloid beta-Protein Precursor, Receptors, Lipoprotein, Protein Transport, LDL-Receptor Related Proteins, Adaptor Proteins, Signal Transducing

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DAB1 and Reelin Effects on Amyloid Precursor Protein and ApoE Receptor 2 Trafficking and Processing

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