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The Journal of Cell Biology, Vol 123, 719-728, Copyright © 1993 by The Rockefeller University Press
ARTICLES |
PB Scotland, M Colledge, I Melnikova, Z Dai and SC Froehner
Department of Physiology, University of North Carolina, Chapel Hill 27599.
A postsynaptic membrane-associated protein of M(r) 43,000 (43-kD protein) is involved in clustering of the nicotinic acetylcholine receptor (AChR) at the neuromuscular junction. Previous studies have shown that recombinant mouse 43-kD protein forms membrane-associated clusters when expressed in Xenopus oocytes. Coexpression with the AChR results in colocalization of the receptor with the 43-kD protein clusters (Froehner, S. C., C. W. Luetje, P. B. Scotland, and J. Patrick, 1990. Neuron. 5:403-410). To understand the mechanism of this clustering, we have studied the role of the carboxy-terminal region of the 43-kD protein. The amino acid sequence of this region predicts two tandem zinc finger structures followed by a serine phosphorylation site. Both Torpedo 43-kD protein and the carboxy-terminal region of the mouse 43-kD protein bind radioisotopic zinc. Mutation of two histidine residues in this predicted domain greatly attenuates zinc binding, lending support to the proposal that this region forms zinc fingers. When expressed in oocytes, the ability of this mutant 43-kD protein to form clusters is greatly reduced. Its ability to interact with AChR, however, is retained. In contrast, a mutation that eliminates the potential serine phosphorylation site has no effect on clustering of the 43-kD protein or on interaction with the AChR. These findings suggest that protein interactions via the zinc finger domain of the 43- kD protein may be important for AChR clustering at the synapse.
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