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• W1520595787 endingPage "29570" @default.
• W1520595787 startingPage "29565" @default.
• W1520595787 abstract "Previous studies have shown that a single type of transmembrane receptor is able to regulate multiple effectors through the activation of heterotrimeric G proteins. For example, the m2 muscarinic acetylcholine receptor (mAChR) expressed in Chinese hamster ovary (CHO) cells inhibits adenylyl cyclase, stimulates phospholipase C-dependent intracellular Ca2+ release, and activates phospholipase A2 through pertussis toxin-sensitive G proteins. However, it is unclear whether multiple effector enzymes can be regulated by one type of heterotrimeric G protein within a single cell. To investigate this question, we constructed a derivative of G alpha i3 (termed G alpha i3 C > S) in which the carboxyl-terminal cysteine residue, the site for pertussis toxin modification, was changed to a serine. Following pertussis toxin treatment of transfected CHO cells expressing the m2 mAChR, we found that the G alpha i3 C > S protein underwent guanine nucleotide exchange in response to the muscarinic agonist carbachol, while the m2 mAChR failed to activate the endogenous G alpha i2 and G alpha i3 proteins. Moreover, coupling of heterotrimeric G proteins containing G alpha i3 C > S to the m2 mAChR resulted in pertussis toxin-resistant inhibition of adenylyl cyclase, stimulation of phospholipase C-induced intracellular Ca2+ release, and phospholipase A2-mediated arachidonic acid release. Therefore, these studies provide conclusive evidence that heterotrimeric G proteins containing just G alpha i3 can regulate multiple effector enzymes within the same cell type." @default.
• W1520595787 created "2016-06-24" @default.
• W1520595787 creator A5017943147 @default.
• W1520595787 creator A5070284483 @default.
• W1520595787 creator A5082548963 @default.
• W1520595787 date "1994-11-01" @default.
• W1520595787 modified "2023-10-15" @default.
• W1520595787 title "Heterotrimeric G proteins containing G alpha i3 regulate multiple effector enzymes in the same cell. Activation of phospholipases C and A2 and inhibition of adenylyl cyclase." @default.
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• W1520595787 doi "https://doi.org/10.1016/s0021-9258(18)43917-8" @default.
• W1520595787 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7961942" @default.
• W1520595787 hasPublicationYear "1994" @default.
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