Direct activation of fission yeast adenylate cyclase by the Gpa2 Gα of the glucose signaling pathway
Direct activation of fission yeast adenylate cyclase by the Gpa2 Gα of the glucose signaling pathway
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DOI：
10.1073/pnas.0502270102
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发表时间：
2005-04-26
影响因子：
11.1
通讯作者：
Hoffman, CS
中科院分区：
文献类型：
--
作者：
Ivey, FD;Hoffman, CS
G 蛋白介导的信号传导涉及酵母和真菌的 cAMP 通路。通过双杂交筛选和下拉实验，我们表明裂殖酵母 Gpa2 G α 结合腺苷酸环化酶的 N 末端结构域，该结构域包含一个与其他真菌腺苷酸环化酶相关性较差的区域内的适度保守的序列。在酵母中过度表达该结构域会扰乱 cAMP 信号传导，而该信号传导可通过 Gpa2 共表达来恢复。影响该结构域（催化结构域超过 1,100 个残基）的突变会改变葡萄糖触发的 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，并表明其激活机制与哺乳动物不同。
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 G alpha 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.