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Direct activation of fission yeast adenylate cyclase by the Gpa2 Gα of the glucose signaling pathway

机译:葡萄糖信号通路的Gpa2Gα直接激活裂变酵母腺苷酸环化酶

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摘要

G protein-mediated signaling is implicated in yeast and fungal cAMP pathways. By two-hybrid screens and pull-down experiments, we show that the fission yeast Gpa2 Gα binds an N-terminal domain of adenylate cyclase, comprising a moderately conserved sequence within a region otherwise poorly related to other fungal adenylate cyclases. Overexpressing this domain in yeast perturbs cAMP signaling, which is restored by Gpa2 coexpression. Mutations affecting this domain, over 1,100 residues from the catalytic domain, alter glucose-triggered cAMP signaling. This is evidence for direct activation of adenylate cyclase by a fungal G protein and suggests a distinct activation mechanism from that of mammals.
机译:G蛋白介导的信号传导与酵母和真菌的cAMP途径有关。通过两次杂交筛选和下拉实验,我们显示裂变酵母Gpa2Gα结合腺苷酸环化酶的N末端结构域,该区域包含一个区域内的中等保守序列,否则该序列与其他真菌腺苷酸环化酶的相关性较差。在酵母中过表达该结构域会干扰cAMP信号传导,该信号可通过Gpa2共表达恢复。影响该结构域的突变(来自催化结构域的1,100多个残基)改变了葡萄糖触发的cAMP信号传导。这是真菌G蛋白直接激活腺苷酸环化酶的证据,并表明了与哺乳动物不同的激活机制。

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