Kim S S, Choi Y M, Suh Y H
Department of Pharmacology, College of Medicine, Seoul National University, Korea.
J Mol Neurosci. 1997 Aug;9(1):49-54. doi: 10.1007/BF02789394.
Mutations in the two related genes, presenilin 1 (PS1) and presenilin 2 (PS2), which are predicted multispanning membrane proteins, are responsible for the majority of early-onset familial Alzheimer's disease (FAD). To demonstrate direct interactions between presenilins (PS) and amyloid precursor protein (APP), the authors utilized a yeast two-hybrid system. Various hydrophilic domains derived from PS and those of APP were coexpressed in yeast and tested for the interaction. No detectable interactions were found in any PS/APP set examined. The authors' studies suggest that PS and APP do not interact through their hydrophilic domains in yeast, raising the possibility that interaction may occur indirectly or require proper conformation or subunit formation.
两个相关基因早老素1（PS1）和早老素2（PS2）发生突变，这两种基因被预测为多跨膜蛋白，是大多数早发性家族性阿尔茨海默病（FAD）的病因。为了证明早老素（PS）与淀粉样前体蛋白（APP）之间的直接相互作用，作者利用了酵母双杂交系统。将源自PS和APP的各种亲水区在酵母中共表达，并检测其相互作用。在所检测的任何PS/APP组合中均未发现可检测到的相互作用。作者的研究表明，在酵母中PS和APP不会通过其亲水区相互作用，这增加了相互作用可能间接发生或需要适当构象或亚基形成的可能性。
