Mouse AChE binds in vivo to domain IV of laminin-1beta.
Functions of acetylcholinesterase (AChE) other than hydrolysis of acetylcholine, e.g. related to cell differentiation, synaptogenesis, neuronal signaling and diseases are well documented, but mechanisms supporting them are not understood. Therefore, we searched for AChE ligands in the central nervous system using a yeast two-hybrid screen (Y2H). 18 independent candidates were identified. One of the membrane or extracellular proteins was laminin-1, an extracellular matrix protein involved in neuronal differentiation and adhesion. The laminin-1 fragment found to interact with AChE contains 898 bp from the 1beta-chain. Moreover, we identified the region containing amino acid residues 240-503 of AChE as essential for interaction with laminin-1beta. Co-immunoprecipitation experiments confirmed the yeast two-hybrid results.
Paraoanu
Laura E
LE
Darmstadt University of Technology, Developmental Biology and Neurogenetics, Schnittspahnstr. 3, D-64287 Darmstadt, Germany.
Layer
Paul G
PG
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism; D007150:Immunohistochemistry; D007797:Laminin / Q000737:chemistry* / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015398:Signal Transduction; D020798:Two-Hybrid System Techniques
D007797:Laminin; C121346:laminin 1; D000110:Acetylcholinesterase