Abstract

An extrinsic membrane protein of apparent molecular mass 43 kDa is specifically localized in postsynaptic membranes closely associated with the nicotinic acetylcholine receptor (AChR). Since its discovery in 1977, biochemical and morphological studies have combined to provide relatively clear pictures of 43K protein structure and subcellular compartmentalization. Nevertheless, despite these advances, the precise function of this synapse-specific protein remains unclear. Data gathered in recent years indicate that the postsynaptic apparatus develops through the incremental agglomeration of receptor microaggregates; evidence derived from a number of sources points to a role for 43K protein in certain underlying reactions. In this paper, I review 43K protein structural and anatomical data and analyze evidence for its role in the organization and maintenance of the postsynaptic membrane. Finally, I offer a model presenting a view of the role of 43K protein in the ontogeny of the motor endplate.

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