Dominant-negative inhibition of pheromone receptor signaling by a single point mutation in the G protein α subunit

Yuh Lin Wu, Shelley B. Hooks, T. Kendall Harden, Henrik G. Dohlman*

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24 引文 斯高帕斯(Scopus)

摘要

In yeast, two different constitutive mutants of the G protein α subunit have been reported. Gpa1Q323L cannot hydrolyze GTP and permanently activates the pheromone response pathway. Gpa1N388D was also proposed to lack GTPase activity, yet it has an inhibitory effect on pheromone responsiveness. We have characterized this inhibitory mutant (designated GαND) and found that it binds GTP, interacts with G protein βγ subunits, and exhibits full GTPase activity in vitro. Although pheromone leads to dissociation of the receptor from wild-type G protein, the same treatment promotes stable association of the receptor with GαND. We conclude that agonist binding to the receptor promotes the formation of a nondissociable complex with GαND, and in this manner prevents activation of the endogenous wild-type G protein. Dominant-negative mutants may be useful in matching specific receptors and their cognate G proteins and in determining mechanisms of G protein signaling specificity.

原文English
頁(從 - 到)35287-35297
頁數11
期刊Journal of Biological Chemistry
279
發行號34
DOIs
出版狀態Published - 20 8月 2004

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