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J Biol Chem, Vol. 274, Issue 29, 20513-20520, July 16, 1999

Altered Glycosylation Sites of the  Subunit of the Acetylcholine Receptor (AChR) Reduce Association and Receptor Assembly

From the Section on Synaptic Mechanisms, Laboratory of Cellular and Molecular Regulation, NIMH, National Institutes of Health, Bethesda, Maryland 20892

We have used mutagenesis to investigate the potential N-glycosylation sites in the  subunit of the mouse muscle acetylcholine receptor (AChR). Of the three sites, Asn⁷⁶, Asn¹⁴³, and Asn¹⁶⁹, only the first two were glycosylated when the  subunit was expressed in COS cells. Because the heterologously expressed  subunit was similar in its properties to that expressed in C2 muscle cells, the sites of glycosylation are likely to be the same in both cases. In COS cells, mutations of the  subunit that prevented glycosylation at either of the sites did not change its metabolic stability nor its steady-state level. These results are in contrast to those found previously for the  subunit, in which glycosylation at a single site metabolically stabilized the polypeptide (Blount, P., and Merlie, J. P. (1990) J. Cell Biol. 111, 2613-2622). Mutations of the  subunit that prevented glycosylation, however, decreased its ability to form an heterodimer when the  and  subunit were expressed together. When all four subunits of the AChR (, , , and ) were coexpressed, mutation of the  subunit to prevent glycosylation resulted in a reduced amount of fully assembled AChR and reduced surface AChR levels, consistent with the role of the heterodimer in the assembly reaction. These results suggest that glycosylation of the  subunit at both Asn⁷⁶ and Asn¹⁴³ is needed for its efficient folding and/or its subsequent interaction with the  subunit.

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