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Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin‐1β
Author(s) -
Paraoanu Laura E.,
Layer Paul G.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.078
Subject(s) - acetylcholinesterase , laminin , complementary dna , microbiology and biotechnology , neurite , extracellular matrix , two hybrid screening , acetylcholine , immunoprecipitation , cell adhesion , yeast , cdna library , cell adhesion molecule , chemistry , adhesion , biochemistry , biology , in vitro , cell , enzyme , gene , endocrinology , organic chemistry
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 heterophilic cell adhesion molecule and searched for proteins interacting 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 β1 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.