Postsynaptic peripheral membrane proteins at the neuromuscular junction have been proposed to participate in the immobilization of the nicotinic acetylcholine receptor at the synapse. An 87 kd cytoplasmic peripheral membrane protein has been demonstrated to colocalize with the nicotinic acetylcholine receptor in the Torpedo electric organ and at the mammalian neuromuscular junction. We have cloned the cDNA encoding the 87K protein from Torpedo electric organ, and the predicted protein sequence is homologous to the C-terminal domains of dystrophin, the protein product of the Duchenne muscular dystrophy gene. The 87K protein displays a restricted pattern of expression detected only in electric organ, brain, and skeletal muscle. Analysis of the in vitro and in vivo phosphorylation of the 87K protein indicates that it is multiply phosphorylated on serine, threonine, and tyrosine residues. The 87K protein is in a complex with other proteins associated with the post-synaptic membrane, including dystrophin and a 58 kd protein. These results suggest that the 87K protein is involved in the formation and stability of synapses and is regulated by protein phosphorylation.
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