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Publication : cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein.

First Author  Bressler SL Year  1996
Journal  Hum Mol Genet Volume  5
Issue  10 Pages  1589-98
PubMed ID  8894693 Mgi Jnum  J:35780
Mgi Id  MGI:83225 Doi  10.1093/hmg/5.10.1589
Citation  Bressler SL, et al. (1996) cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein. Hum Mol Genet 5(10):1589-98
abstractText  Using the yeast two hybrid system, a mouse embryo cDNA library was screened for proteins that interact with the C- terminus of the human beta-amyloid precursor protein (PPP), A fusion protein was identified that interacts specifically with the cytoplasmic domain of PPP and does not interact with the beta-amyloid region, The protein encoded by this partial mouse cDNA is identical to the C- terminus of the rat Fe65 protein, This mouse protein also interacts with the homologous C-terminal domains of the mouse amyloid precursor-like proteins, APLP1 and APLP2, These conserved cytoplasmic regions contain a common amino acid motif, Asn-Pro-Thr-Tyr, which has previously been shown to influence both the secretion and internalization of PPP. Fe65 has been implicated in regulatory and cell signaling mechanisms because it contains two different motifs involved in protein binding, a WW domain (a variant of Src homology 3 domains) and a phosphotyrosine interaction domain (PID). Interestingly, the PID domain binds to the same motif present in the conserved cytoplasmic domains of the PPP and PPP-like proteins, RNA analyses reveal that Fe65 is predominantly expressed in brain and in the regions most affected by Alzheimer's disease (AD)-associated neuropathology, The human Fe65 mRNA was cloned from a fetal brain cDNA library. The message encodes a protein of 735 amino acids that is 95% identical to the rat Fe65 protein. The human Fe65 gene was mapped on human metaphase chromosomes to band 11p15 using fluorescence in situ hybridization.
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