Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1β
Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1β
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DOI：
10.1016/j.febslet.2004.08.078
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发表时间：
2004-10-08
期刊：
影响因子：
3.5
通讯作者：
Layer, PG
中科院分区：
文献类型：
--
作者：
Paraoanu, LE;Layer, PG
乙酰胆碱酯酶（AChE）可能具有除水解乙酰胆碱以外的作用，例如，与神经突生长、分化和粘附等发育过程相关。在此，我们研究了AChE是否可以作为一个heteropholic细胞粘附分子，并寻找与之相互作用的蛋白质，使用酵母双杂交方法和小鼠脑cDNA文库，我们已经确定了编码层粘连蛋白链β 1的球状结构域IV的部分cDNA与小鼠AChE的氨基酸240-503之间的相互作用。生化免疫共沉淀试验证实了遗传结果。我们认为，乙酰胆碱酯酶，通过与层粘连蛋白-1相互作用，是能够施加粘附信号通路的变化。(C)2004年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
Acetylcholinesterase (AChE) is likely to have roles other than the hydrolysis of acetylcholine, e.g., related to developmental processes like neurite outgrowth, differentiation and adhesion. Here, we investigated whether AChE can function as a heteropholic cell adhesion molecule and searched for proteins interacting is with it. Using the yeast two-hybrid method and a mouse brain cDNA library, we have identified an interaction between a partial cDNA encoding the globular domain IV of laminin chain beta1 and the amino acids 240-503 of mouse AChE. Biochemical co-immunoprecipitation assays confirmed the genetic results. We suggest that AChE, by interacting with laminin-1, is able to exert changes in adhesion signaling pathways. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.