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Vol. 61, Issue 1, 150-159, January 2002
10, That Confers
Functionality to the 9-Subunit
Sanofi-Synthélabo, Department of Molecular and Functional
Genomics, Rueil-Malmaison, France (F.S., E.C., N.W., D.C., D.G., F.B.);
and Department of Physiology, Centre Médical Universitaire,
Geneva, Switzerland (E.C., S.B., D.B.)
We present herein the cloning of the human nicotinic acetylcholine
receptor 
9-ortholog and the identification of a new -like subunit
(10) that shares 58% identity with 9. Whereas 10 fails to
produce functional receptors alone, it promoted robust
acetylcholine-evoked currents when coinjected with 9. The presence
of 10 modifies the physiological and pharmacological properties of
the 9 receptor indicating that the two subunits coassemble in a
single functional receptor. Fusing the N-terminal domain of 9 with
the rest of the 10-cDNA yielded a functional 9:10-chimera that
displays the acetylcholine binding properties of 9 and ionic pore
characteristics of 10-containing receptors. In addition, 9- and
10-subunit mRNAs show limited similar tissue distribution patterns
and are expressed in cochlea, pituitary gland, and keratinocytes. These data suggest that, in vivo, 9-containing receptors coassemble with
10-subunit.
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