Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1beta.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Paraoanu LE,Layer PG

doi

10.1016/j.febslet.2004.08.078

keywords:

subject

Has Abstract

pub_date

2004-10-08 00:00:00

pages

161-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014579304011159

journal_volume

576

pub_type

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