Froehner_1989_FEBS.Lett_249_229

A cDNA clone encoding the mouse muscle postsynaptic 43 kDa protein was isolated and sequenced. The amino acid sequence of this protein, which is closely associated with nicotinic acetylcholine receptors at Torpedo electrocyte and vertebrate skeletal muscle synapses, is very similar in different species. A cysteine-rich region homologous to part of the regulatory domain of protein kinase C may be important in interactions of this protein with the lipid bilayer. RNA transcripts for the 43 kDa protein increase only 2-3 fold after denervation of rat skeletal muscle, in sharp contrast to the alpha-subunit of the muscle nicotinic receptor which increases more than 30-fold. Thus, the expression of these two proteins is regulated by different mechanisms.