The muscarinic acetylcholine receptors (mAChR) mediate a variety of cellular responses, including inhibition of adenylate cyclase, brea own of phosphoinositides and modulation of potassium channels. The mAChRs transduce signals by coupling to G-proteins, which then modulate several downstream effector proteins and ion channels. Five mAChR subtypes have been identified, designated M1 to M5. The five receptor subtypes show distinct patterns of tissue distribution, as well as distinct pharmacological and functional properties. The amino acid sequence of each mAChR subtype reflects a structure that is characteristic of G-protein coupled receptors, consisting of seven highly conserved transmembrane segments and a large intracellular region unique to each subtype, which constitutes the effector-coupling domain.