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The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein
Open accessAbstract
Fe65 is a protein mainly expressed in several districts of the mammalian nervous system. The search of protein sequence data banks revealed that Fe65 contains two phosphotyrosine interaction (PID) or phosphotyrosine binding (PTB) domains, previously identified in the Shc adaptor molecule. The two putative PID/PTB domains of Fe65 were used to construct glutathione S-transferase-Fe65 fusion proteins. Co-precipitation experiments demonstrated that the Fe65 PID/PTB domains interacted with several proteins of apparent molecular mass 135, 115, 105, and 51 kDa. The region of Fe65 containing the PID/PTB domains was used as a bait to screen a human brain cDNA library in yeast by the two-hybrid system. Three different cDNA clones were isolated, two of which contain overlapping segments of the cDNA encoding the COOH terminus of the Alzheimer's beta-amyloid-precursor protein (APP), that represents the short intracellular domain of this membrane protein. The third clone contains a cDNA fragment coding for the COOH terminus of the human counterpart of a mouse beta-amyloid-like precursor protein. The alignment of the three APP encoding cDNA fragments found in the screening suggests that the region of APP involved in the binding is centered on the NPTY sequence, which is analogous to that present in the intracellular domains of the growth factor receptors interacting with the PID/PTB domain of Shc.
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“Intracellularly, APP and ApoER2 bind the adaptor proteins X11␣/ (67-70), Fe65 (69, 71, 72), Snx17 (73, 74), Dab1 (75-79), and Dab2 (73, 80), and these interactions regulate their surface expression and processing (Fig. 4).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [71]
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Metadata
- Authors
- Fiore, F., Zambrano, N., Minopoli, G., Donini, V., Duilio, A., & Russo, T.
- Affiliations
- University of Naples Federico II (IT)
- Corresponding author
- Russo, Tommaso
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 270
- Issue
- 52
- Pages
- 30853-30856
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2087496042
- Cited by
- 294
- References
- 37
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 6 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 7 · 2016: 4 · 2015: 3 · 2014: 5 · 2013: 8 · 2012: 10
- FWCI
- 9.48
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Fe65, phosphotyrosine binding domain, Shc, amyloid precursor protein, APP intracellular domain, protein-protein interaction, yeast two-hybrid screen, GST fusion protein, Alzheimer's disease
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Nuclear Proteins, Protein Binding, Amyloid beta-Protein Precursor, PC12 Cells, Sequence Homology, Amino Acid, DNA, Complementary, src Homology Domains, Phosphotyrosine, Mice, Rats
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