Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1beta.
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 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.
Technical University Darmstadt, Institute of Zoology, Department of Developmental Biology and Neurogenetics, Schnittspahnstr. 3, 64287 Darmstadt, Germany.
Laura E
LE
Paraoanu
Paul G
PG
Layer
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism; D015153:Blotting, Western; D002460:Cell Line; D005109:Extracellular Matrix / Q000737:chemistry*; D015723:Gene Library; D006801:Humans; D007797:Laminin / Q000378:metabolism*; D051379:Mice; D011233:Precipitin Tests; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D000911:Antibodies, Monoclonal; D007797:Laminin; C121346:laminin 1; D000110:Acetylcholinesterase