TAILIEUCHUNG - Báo cáo khoa học: Activation of nematode G protein GOA-1 by the human muscarinic acetylcholine receptor M2 subtype Functional coupling of G-protein-coupled receptor and G protein originated from evolutionarily distant animals

Signal transduction mediated by heterotrimeric G proteins regulates a wide variety of physiological functions. We are interested in the manipulation of G-protein-mediating signal transduction using G-protein-coupled receptors, which are derived from evolutionarily distant organisms and recognize unique ligands. | ễFEBS Journal Activation of nematode G protein GOA-1 by the human muscarinic acetylcholine receptor M2 subtype Functional coupling of G-protein-coupled receptor and G protein originated from evolutionarily distant animals Masaomi Minaba1 Susumu Ichiyama2 Katsura Kojima3 Mamiko Ozaki4 and Yusuke Kato1 1 Immune Defense Unit National institute of AgrobiologicalSciences Ibaraki Japan 2 Institute for Biomolecular Science Faculty of Science Gakushuin University Tokyo Japan 3 Silk-Materials Research Unit National institute of AgrobiologicalSciences Ibaraki Japan 4 Department of Biology Faculty of Science Kobe University Japan Keywords biotechnology Caenorhabditis elegans G protein muscarinic acetylcholine receptor nematodes Correspondence Y. Kato Immune Defense Unit National Institute of AgrobiologicalSciences Tsukuba Ibaraki 305-8634 Japan Fax Tel 81 29 838 6059 E-mail kato@ Received 18 August 2006 revised 12 October 2006 accepted 17 October 2006 doi Signal transduction mediated by heterotrimeric G proteins regulates a wide variety of physiological functions. We are interested in the manipulation of G-protein-mediating signal transduction using G-protein-coupled receptors which are derived from evolutionarily distant organisms and recognize unique ligands. As a model we tested the functionally coupling GOA-1 Gai o ortholog in the nematode Caenorhabditis elegans with the human muscarinic acetylcholine receptor M2 subtype M2 which is one of the mammalian Gai o-coupled receptors. GOA-1 and M2 were prepared as a fusion protein using a baculovirus expression system. The affinity of the fusion protein for GDP was decreased by addition of a muscarinic agonist carbamylcholine and the guanosine 5 - 3-ơ-thio triphosphate 35S GTPyS binding was increased with an increase in the carbamylcholine concentrations in a dosedependent manner. These effects evoked by carbamylcholine were completely abolished by a full antagonist atropine. In .

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