The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine‐binding domain proteins in the yeast two‐hybrid system

FEBS Letters

M. McLoughlin, Declan¹  C.J. Miller, Christopher¹ 

[1] Department of Neurology, The Institute of Psychiatry, De Crespigny Park, Denmark Hill, London SE5 8AF, UK

关键词: APP;    Alzheimer's disease;    Fe65;    X11;    Phosphotyrosine-binding domain;   

DOI  :  10.1016/S0014-5793(96)01128-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have used the yeast two-hybrid system to screen for proteins that interact with the carboxy-terminal domain of APP. Six different clones were isolated and sequence analyses revealed that they encoded domains of a previously described neuronal protein Fe65, a homologue of Fe65 and a homologue of protein X11. All of these proteins contain one or more phosphotyrosine binding (PTB) domains. PTB domain proteins bind to the sequence Asn-Pro-X-Tyr when the Tyr is phosphorylated and are believed to function in signal transduction. APP contains such a motif. These results are consistent with a role for APP in signal transduction mechanisms.

【 授权许可】

Unknown