Journal
MOLECULAR AND CELLULAR NEUROSCIENCE
Volume 46, Issue 1, Pages 272-281Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.mcn.2010.09.010
Keywords
Acetylcholinesterase; Acetylcholine; Collagen Q; PRiMA; Synapse structure; Electron microscopy; Muscle activity
Categories
Funding
- National Institutes of Health [P42-ES010337, R37-GM18360-35]
- Inserm
- Association Francaise contre les Myopathies (AFM)
- Agence Nationale de la Recherche (ANR Neuroscience)
- Bonus Quake Recherche Universite Paris Descartes
- Centre National de la Recherche Scientifique (CNRS)
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Acetylcholinesterase (AChE) terminates the action of acetylcholine at cholinergic synapses thereby preventing rebinding of acetylcholine to nicotinic postsynaptic receptors at the neuromuscular junction. Here we show that AChE is not localized close to these receptors on the postsynaptic surface, but is instead clustered along the presynaptic membrane and deep in the postsynaptic folds. Because AChE is anchored by ColQ in the basal lamina and is linked to the plasma membrane by a transmembrane subunit (PRiMA), we used a genetic approach to evaluate the respective contribution of each anchoring oligomer. By visualization and quantification of AChE in mouse strains devoid of ColQ PRiMA or AChE, specifically in the muscle, we found that along the nerve terminus the vast majority of AChE is anchored by ColQ that is only produced by the muscle, whereas very minor amounts of AChE are anchored by PRiMA that is produced by motoneurons. In its synaptic location, AChE is therefore positioned to scavenge ACh that effluxes from the nerve by non-quantal release. AChE-PRiMA, produced by the muscle, is diffusely distributed along the muscle in extrajunctional regions. (C) 2010 Elsevier Inc. All rights reserved.
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