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XB-ART-13012
J Cell Biol May 17, 1999; 145 (4): 911-21.

Acetylcholinesterase clustering at the neuromuscular junction involves perlecan and dystroglycan.

Peng HB , Xie H , Rossi SG , Rotundo RL .


Abstract
Formation of the synaptic basal lamina at vertebrate neuromuscular junction involves the accumulation of numerous specialized extracellular matrix molecules including a specific form of acetylcholinesterase (AChE), the collagenic-tailed form. The mechanisms responsible for its localization at sites of nerve- muscle contact are not well understood. To understand synaptic AChE localization, we synthesized a fluorescent conjugate of fasciculin 2, a snake alpha-neurotoxin that tightly binds to the catalytic subunit. Prelabeling AChE on the surface of Xenopus muscle cells revealed that preexisting AChE molecules could be recruited to form clusters that colocalize with acetylcholine receptors at sites of nerve-muscle contact. Likewise, purified avian AChE with collagen-like tail, when transplanted to Xenopus muscle cells before the addition of nerves, also accumulated at sites of nerve-muscle contact. Using exogenous avian AChE as a marker, we show that the collagenic-tailed form of the enzyme binds to the heparan-sulfate proteoglycan perlecan, which in turn binds to the dystroglycan complex through alpha-dystroglycan. Therefore, the dystroglycan-perlecan complex serves as a cell surface acceptor for AChE, enabling it to be clustered at the synapse by lateral migration within the plane of the membrane. A similar mechanism may underlie the initial formation of all specialized basal lamina interposed between other cell types.

PubMed ID: 10330416
PMC ID: PMC2133180
Article link:
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: ache actl6a dag1 hspg2


Article Images: [+] show captions
References [+] :
Anderson, Fluorescent staining of acetylcholine receptors in vertebrate skeletal muscle. 1974, Pubmed