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Volume 271, Number 44, Issue of November 1, 1996 pp. 27575-27584
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Assembly of the Nicotinic Acetylcholine Receptor
THE FIRST TRANSMEMBRANE DOMAINS OF TRUNCATED  AND  SUBUNITS ARE REQUIRED FOR HETERODIMER FORMATION IN VIVO

(Received for publication, May 29, 1996, and in revised form, August 7, 1996)

Zuo-Zhong Wang ^§ , Stephen F. Hardy and Zach W. Hall ^§

From the  Department of Physiology, University of California, San Francisco, California 94143 and the ^§ Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, Maryland 20892

To investigate the mechanism of assembly of the mouse muscle acetylcholine receptor, we have expressed truncated N-terminal fragments of the  and  subunits in COS cells and have examined their ability to fold, to associate into heterodimers, and to form a ligand-binding site. Truncated fragments of the  subunit that include all, part, or none of the first transmembrane domain (M1) folded to acquire -bungarotoxin binding activity. Neither the full-length  subunit nor any of the fragments were expressed on the cell surface, although the shortest folded fragment lacking a transmembrane domain was secreted into the medium. When coexpressed with the  subunit, the  subunit fragment possessing M1 formed a heterodimer containing a ligand-binding site, but shorter fragments, which lack transmembrane segments, did not associate with the  subunit. N-terminal  subunit fragments gave similar results. An N-terminal  subunit fragment that contains M1 associated with the  subunit to form a heterodimer, while a fragment lacking M1 did not. These results show that a complete M1 domain is necessary for association of truncated N-terminal  and  subunits into a heterodimer with high affinity ligand binding activity.

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