Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's β-amyloid precursor protein

@article{Tanahashi1999MolecularCO,
  title={Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's $\beta$-amyloid precursor protein},
  author={Hiroshi Tanahashi and Takeshi Tabira},
  journal={Neuroscience Letters},
  year={1999},
  volume={261},
  pages={143-146}
}
Genome structure and chromosomal mapping of the gene for Fe65L2 interacting with Alzheimer's beta-amyloid precursor protein.
TLDR
The entire genome structure and the chromosomal mapping of the Fe65L2 gene are reported, which will be useful in the linkage analysis and search for mutations in theFe65L1 gene in patients with Alzheimer's disease.
The FE65 proteins and Alzheimer's disease
TLDR
The known functions of the FE65 family are reviewed and their role in APP function and Alzheimer's disease is reviewed, finding that APPs, FE65s, and mena may act together in a developmental signalling pathway.
Cytosolic protein‐protein interactions that regulate the amyloid precursor protein
TLDR
Data revealing which proteins bind to the cytoplasmic domain of APP is discussed, how these binding‐proteins regulate APP metabolism and function, and why such protein‐protein interactions provide an exciting new target for therapeutic intervention in AD are discussed.
C-terminal 37 residues of LRP promote the amyloidogenic processing of APP independent of FE65
TLDR
It is demonstrated that the last 37 residues of LRP cytoplasmic tail (LRP‐C37) lacking the NPxY motifs and FE65 binding mediate the core pro‐amyloidogenic activity of L RP‐ST.
Fe65 and X11beta co-localize with and compete for binding to the amyloid precursor protein.
TLDR
It is shown that in neurones and transfected cells, APP, Fe65 and X11beta show overlapping subcellular distributions and it is demonstrated that Fe65AndX11beta compete for binding to APP.
A candidate molecular mechanism for the association of an intronic polymorphism of FE65 with resistance to very late onset dementia of the Alzheimer type.
TLDR
Evidence is shown that an attenuated binding of FE65 with betaPP is, in part, responsible for resistance to the very late onset disease, and sequence analysis of the FE65 of mice, non-human primates and man revealed that the susceptibility allele was favored by natural selection leading to the authors' lineage.
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References

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Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein.
TLDR
The cloning of another Fe65-like cDNA (Fe65L2), similar to Fe65 and to Fe 65L1, which encodes a protein of approx.
Isolation and characterization of APLP2 encoding a homologue of the Alzheimer's associated amyloid β protein precursor
TLDR
It is shown that APLP2 is a close relative of APP and exhibits a very similar pattern of expression in the brain and throughout the body and contains a cytoplasmic domain predicted to couple with the GTP–binding protein Go indicating that it may be an additional cell surface activator of this G protein.
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 (*)
TLDR
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.
APP-BP1, a Novel Protein That Binds to the Carboxyl-terminal Region of the Amyloid Precursor Protein (*)
TLDR
The cloning of a cDNA encoding a ubiquitously expressed 59-kDa APP-binding protein, called APP-BP1, is 61% similar to a protein encoded by the Arabidopsis AXR1 gene, required for normal response to the hormone auxin, and is a relative of the ubiquitin activating enzyme E1.
The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type
TLDR
The interaction of FE65 with βPP and the association of a FE65 polymorphism with DAT lend credence to the hypothesis that the metabolism of βPP is central to the pathogenesis of common sporadic forms of DAT.
Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein.
TLDR
The existence of a human FE65 gene family and evidence supporting specific interactions between members of the beta PP and FE65 protein families are reported and sequence analysis of the FE65 human gene family reveals the presence of two phosphotyrosine interaction (PI) domains.
Interaction of the Phosphotyrosine Interaction/Phosphotyrosine Binding-related Domains of Fe65 with Wild-type and Mutant Alzheimer's β-Amyloid Precursor Proteins*
TLDR
A role for Fe65 in the pathogenesis of familial Alzheimer's disease is suggested by the finding that mutant APP shows an altered in vivo interaction with Fe65, as demonstrated by anti-Fe65 co-immunoprecipitation experiments.
The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
TLDR
The X11 PI domain binds a YENPTY motif in the intracellular domain of (beta)APP that is strikingly similar to the NPXY motifs that bind the Shc and IRS-1 PI/PTB domains.
Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid beta protein precursor.
TLDR
Data indicate that the APP gene is a member of a strongly conserved gene family and studies aimed at determining the functions of the proteins encoded by this gene family should provide valuable clues to their potential role in Alzheimer disease neuropathology.
The Fe65 Adaptor Protein Interacts through Its PID1 Domain with the Transcription Factor CP2/LSF/LBP1*
TLDR
Co-immunoprecipitation experiments demonstrated that the interaction between Fe65 and CP2/LSF/LBP1 also takes place in vivo between the native molecules and a small region N-terminal to the WW domain is phosphorylated and is necessary for the presence of Fe65 in the nuclear fraction.
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