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 pro...
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| Veröffentlicht in: | FEBS letters 2004-10, Vol.576 (1-2), p.161-164 |
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| creator | Paraoanu, Laura E Layer, Paul G |
| description | 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. |
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| ispartof | FEBS letters, 2004-10, Vol.576 (1-2), p.161-164 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; ScienceDirect Journals (5 years ago - present); Alma/SFX Local Collection |
| subjects | Acetylcholinesterase - metabolism Animals Antibodies, Monoclonal - metabolism Blotting, Western Cell Line Extracellular Matrix - chemistry Gene Library Humans Laminin - metabolism Mice Precipitin Tests Saccharomyces cerevisiae - metabolism Two-Hybrid System Techniques |
| title | Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1beta |
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