The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
DAB1 and Reelin Effects on Amyloid Precursor Protein and ApoE Receptor 2 Trafficking and Processing
Open accessAbstract
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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In the citing paper
“There is also evidence showing that reelin induces ApoER2 processing [42], [43] and degradation [43], however the mechanisms by which this is accomplished by reelin is not completely clear.”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [42]
In the citing paper
“Several lines of evidence relate ApoER2 trafficking with its susceptibility to proteolytic processing by the α-secretases of the ADAM family and by the γ-secretase complex [39], [42], [55], [57].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [42]
In the citing paper
“Interestingly, some of these proteins also regulate the proteolytic processing of this receptor [42], [54], [55], [66] by binding to its NPxY motif.”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [42]
In the citing paper
“Reduced Reelin expression in HRM mice exacerbates the accumulation of both A and phosphorylated tau (94), whose production is inhibited by Reelin signaling (Ref.76 and reviewed in Ref. 31).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [76]
Citations
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Research works printed but not linked: 1
- Parisiadou, 2006, Neurobiol. Aging
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Reelin, lipoprotein receptors and synaptic plasticity
Herz, J., & Chen, Y. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn2009 · Cited by 524
Young-Pearse, T. L., Bai, J., Chang, R., Zheng, J. B., LoTurco, J. J., & Selkoe, D. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4701-07.2007 · Cited by 369
Substrate specificity of γ-secretase and other intramembrane proteases
Beel, A. J., & Sanders, C. R. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7462-2 · Cited by 274
The Reelin signaling pathway promotes dendritic spine development in hippocampal neurons
Niu, S., Yabut, O., & D'Arcangelo, G. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.1917-08.2008 · Cited by 266
Interaction of Reelin with Amyloid Precursor Protein Promotes Neurite Outgrowth
Hoe, H.-S., Lee, K. J., Carney, R. S. E., Lee, J., Markova, A., Lee, J.-Y., Howell, B. W., Hyman, B. T., Pak, D. T. S., Bu, G., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4872-08.2009 · Cited by 219
Self-citation
Metadata
- 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
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-11
- Volume
- 281
- Issue
- 46
- Pages
- 35176-35185
- ISSN
- 0021-9258 (ISSN-L)
- 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
- 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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