Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid.

@article{Ando2001PhosphorylationdependentRO,
  title={Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid.},
  author={Katsuyuki Ando and K I Iijima and James I. Elliott and Yutaka Kirino and Toshiharu Suzuki},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 43},
  pages={40353-61}
}
Neuronal Fe65 is an adapter protein that interacts with the cytoplasmic domain of the beta-amyloid precursor protein (APP). Although the interaction has been reported to occur between the second phosphotyrosine interaction domain of Fe65 and the YENPTY motif in the cytoplasmic domain of APP, the regulatory mechanism and biological function of this interaction remain unknown. We report here that (i) a single amino acid mutation at the Thr-668 residue of APP695, located 14 amino acids toward the… CONTINUE READING
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