Abstract
The proper organization of acetylcholinesterase (AChE) molecules at the neuromuscular synapse is essential for terminating neurotransmission by rapidly hydrolysing acetylcholine. To provide for this organization, a highly specialized mechanism must exist to insure that the appropriate numbers of AChE molecules are produced at the synapse and that they are targeted and attached specifically to the synaptic basal lamina interposed between the nerve terminal and the postsynaptic membrane. Work from our laboratory has previously shown that AChE molecules in tissue-cultured skeletal muscle fibers are locally synthesized, transported, and organized in discreet domains on the muscle cell surface. These studies provided the basis for understanding events at the adult neuromuscular synapse where local accumulation of AChE transcripts can insure increased local synthesis of AChE, and specific receptors on the synaptic basal lamina exist which can bind and retain the collagen-tailed form of AChE.
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© 1998 Springer Science+Business Media New York
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Rotundo, R.L., Rossi, S.G., Pu, H., Peng, H.B. (1998). Fluorescent Fasciculin. In: Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. (eds) Structure and Function of Cholinesterases and Related Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1540-5_9
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DOI: https://doi.org/10.1007/978-1-4899-1540-5_9
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