Abstract
We present herein the cloning of the human nicotinic acetylcholine receptor α9-ortholog and the identification of a new α-like subunit (α10) that shares 58% identity with α9. Whereas α10 fails to produce functional receptors alone, it promoted robust acetylcholine-evoked currents when coinjected with α9. The presence of α10 modifies the physiological and pharmacological properties of the α9 receptor indicating that the two subunits coassemble in a single functional receptor. Fusing the N-terminal domain of α9 with the rest of the α10-cDNA yielded a functional α9:α10-chimera that displays the acetylcholine binding properties of α9 and ionic pore characteristics of α10-containing receptors. In addition, α9- and α10-subunit mRNAs show limited similar tissue distribution patterns and are expressed in cochlea, pituitary gland, and keratinocytes. These data suggest that, in vivo, α9-containing receptors coassemble with α10-subunit.
- The American Society for Pharmacology and Experimental Therapeutics
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