Compartmentalization of Acetylcholine Receptor Gene Expression during Development of the Neuromuscular Junction
This extract was created in the absence of an abstract.
Excerpt
The nicotinic acetylcholine receptor (AChR) is a membrane-bound allosteric protein engaged in intercellular communication at the cholinergic synapse. This transmembrane heterologous (α2 β γ δ) pentamer operates in the millisecond time scale as an acetylcholine-gated cationic channel, and its functional architecture is actively investigated (Changeux 1981; Popot and Changeux 1984; Hucho 1986; Lindstrom et al. 1987; and this volume). In particular, the regions of the molecule that form its two main functional domains, namely, the acetylcholine-binding site and the agonist-gated ion channel, have recently been defined at the amino acid level (for review, see Changeux 1990; Galzi et al. 1990).
The AChR protein is also a dominant component of the postsynaptic membrane of the motor endplate. In the adult, the density of AChR under the motor nerve ending reaches approximately 10,000 molecules per μm2 and drops more thatn 1000-fold only a few micrometers away (for review, see Salpeter and Loring...
