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Journal of Neuroscience, Vol 14, 785-795, Copyright © 1994 by Society for Neuroscience
The role of the cytoplasmic domains of individual subunits of the acetylcholine receptor in 43 kDa protein-induced clustering in COS cells
XM Yu and ZW Hall
Department of Physiology, University of California at San Francisco 94143-0444.
The 43 kDa protein, a cytoplasmic peripheral membrane protein, is closely
associated with the acetylcholine receptor (AChR) at the neuromuscular
junction, where it is thought to anchor the receptor in the postsynaptic
membrane. We have used the 43 kDa protein-induced clustering of AChRs that
occurs when both proteins are transiently expressed in COS cells to
investigate which parts of the AChR might interact with the 43 kDa protein.
By constructing chimeric subunits, we showed that the cytoplasmic domains
of neither the epsilon nor delta subunits are required for 43 kDa
protein-induced clustering. Systematic mutational analysis of the long
cytoplasmic loops of the alpha and beta subunits showed that most of the
loops can be altered without affecting the ability of the AChR to be
clustered; in each case, however, one or more sequences could not be
tested, because mutation in these regions prevented AChR assembly. Our
results suggest either that these regions are involved in clustering or
that the 43 kDa protein can interact with multiple, alternative sites on
the cytoplasmic surface of the AChR. Our experiments also show that the
postulated sites of tyrosine phosphorylation in the beta subunit and of
serine phosphorylation in the alpha subunit can be mutated without
affecting 43 kDa protein- induced AChR clustering.
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