Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1.
Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1.
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DOI：
10.1038/ncomms7975
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发表时间：
2015-04-21
影响因子：
16.6
通讯作者：
Saito H
中科院分区：
文献类型：
--
作者：
Tatebayashi K;Yamamoto K;Nagoya M;Takayama T;Nishimura A;Sakurai M;Momma T;Saito H
酵母高渗透压甘油（HOG）途径激活Hog1 MAP激酶，协调对高渗透压条件的适应。在这里，我们证明了四跨膜（TM）结构域蛋白Sho1是HOG途径HKR1亚分支的渗透传感器。交联研究表明，Sho1通过在TM1/TM4界面二聚和在TM2/TM3界面三聚形成二聚体-三聚体结构的平面低聚物。高外部渗透压诱导Sho1 TM结构域的结构变化和Sho1与细胞质接头蛋白Ste50的结合，从而导致Hog1激活。除了它的渗透功能外，Sho1寡聚物还起到支架的作用。Sho1通过分别在TM1/TM4和TM2/TM3界面与TM蛋白Opy2和Hkr1结合，形成了Hog1激活所必需的多组分信号复合物。我们的研究结果阐明了Sho1的四个TM结构域如何决定低聚物结构及其渗透和支架功能。酵母高渗透压甘油途径通过SLN1和SHO两个分支激活Hog1 MAP激酶，但渗透传感器的身份仅在SLN1分支上得到证实。在这里，作者证明了4 - tm结构域蛋白Sho1既是渗透传感器又是Hog1激活所必需的衔接蛋白。
The yeast high osmolarity glycerol (HOG) pathway activates the Hog1 MAP kinase, which coordinates adaptation to high osmolarity conditions. Here we demonstrate that the four-transmembrane (TM) domain protein Sho1 is an osmosensor in the HKR1 sub-branch of the HOG pathway. Crosslinking studies indicate that Sho1 forms planar oligomers of the dimers-of-trimers architecture by dimerizing at the TM1/TM4 interface and trimerizing at the TM2/TM3 interface. High external osmolarity induces structural changes in the Sho1 TM domains and Sho1 binding to the cytoplasmic adaptor protein Ste50, which leads to Hog1 activation. Besides its osmosensing function, the Sho1 oligomer serves as a scaffold. By binding to the TM proteins Opy2 and Hkr1 at the TM1/TM4 and TM2/TM3 interface, respectively, Sho1 forms a multi-component signalling complex that is essential for Hog1 activation. Our results illuminate how the four TM domains of Sho1 dictate the oligomer structure as well as its osmosensing and scaffolding functions. The yeast high osmolarity glycerol pathway activates the Hog1 MAP kinase via two branches, SLN1 and SHO, but the identity of the osmosensor has only been shown for the SLN1 branch. Here the authors demonstrate that the four-TM domain protein Sho1 functions as both an osmosensor and adaptor protein necessary for Hog1 activation.
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