A cDNA clone encoding a muscarinic acetylcholine receptor (mAChR) has been obtained from the nematode Caenorhabditis elegans. The nematode mAChR, consisted of 585 amino acids, reveals a high degree of amino acid identity to other previously known mACh...
A cDNA clone encoding a muscarinic acetylcholine receptor (mAChR) has been obtained from the nematode Caenorhabditis elegans. The nematode mAChR, consisted of 585 amino acids, reveals a high degree of amino acid identity to other previously known mAChRs. Excluding a highly variable middle portion of the third intracellular loop, the C. elegans mAChR shared about 51% amino acid identity with a Drosophila mAChR and 42-44% identity with human m1-m5 mAChR subtypes. When stably expressed in CHO cells, the C. elegans mAChR exhibited a high affinity binding for N-[^3H]methylscopolamine ([^3H]NMS). This [^3H]NMS binding was competitively inhibited by classical muscarinic ligands such as atropine and oxotremorine. These data demonstrate the functional expression of the C. elegans mAChR in CHO cells. Activation of the C. elegans mAChR with carbachol resulted in the stimulation of phosphatidylinositol metabolism in CHO cells, suggesting that the receptor is coupled to phospholipase C activation.