Carboxyl-terminal mutations of Gq alpha and Gs alpha that alter the fidelity of receptor activation.

白细胞介素5受体α亚单位 Gα亚单位 白细胞介素10受体,α亚单位 受体 阿尔法(金融) 半胱氨酸环受体 G蛋白 氨基酸 腺苷酸环化酶 G蛋白偶联受体 Gqα亚单位 生物化学 生物
作者
Bruce R. Conklin,Paul Herzmark,S. Ishida,Tatyana A. Voyno-Yasenetskaya,Ying Sun,Zvi Farfel,Henry R. Bourne
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期刊:PubMed 卷期号:50 (4): 885-90 被引量:39
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The carboxyl terminus of the G protein alpha subunit is a key determinant of the fidelity of receptor activation. We have previously shown that the Gq alpha subunit (alpha q) can be made to respond to alpha i-coupled receptors by replacing its carboxyl terminus with the corresponding alpha i2, alpha o, alpha z residues. We now extend these findings in three ways: 1) carboxyl-terminal mutations of alpha q/alpha i chimeras show that the critical amino acids are in the -3 and -4 positions, 2) exchange of carboxyl termini between alpha q and alpha z allows activation by receptors appropriate to the carboxyl-terminal residues, and 3) we identify receptors that either do or do not activate the expected carboxyl-terminal chimeras (alpha q/alpha i, alpha q/alpha s, alpha s/alpha q). Replacement of the five carboxyl-terminal amino acids of alpha q with the alpha s sequence permitted an alpha s-coupled receptor (the V2 vasopressin receptor but not the beta 2-adrenergic receptor) to stimulate phospholipase C. Replacement of the five carboxyl-terminal amino acids of alpha z with residues of alpha q permitted certain alpha q-coupled receptors (bombesin and V1a vasopressin receptors but not the oxytocin receptor) to stimulate adenylyl cyclase. Thus, the relative importance of the G alpha carboxyl terminus in permitting coupling to a new receptor depends on the receptor with which it is paired. These studies refine our understanding and provide new tools with which to study the fidelity of receptor/G alpha activation.

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