The N-terminal acidic residue of the cytosolic helix 8 of an odorant receptor is responsible for different response dynamics via G-protein
The N-terminal acidic residue of the cytosolic helix 8 of an odorant receptor is responsible for different response dynamics via G-protein
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DOI：
10.1016/j.febslet.2015.03.025
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发表时间：
2015-04-28
期刊：
影响因子：
3.5
通讯作者：
Sato, Takaaki
中科院分区：
文献类型：
--
作者：
Kawasaki, Takashi;Saka, Takahiro;Sato, Takaaki
我们之前观察到小鼠嗅觉受体S6(MOR-S6)与嵌合Gα(15)_(Olf)的反应非常迅速和强大，而Gα(15)则是如此。为了确定导致这种反应差异的残基，我们在一个异源功能表达系统中分析了胞浆螺旋8的突变。MOR-S6的螺旋8和TM1-2之间的N末端疏水核心对Gα(15)_(Olf)和Gα(15)的激活都是重要的。螺旋8N末端酸性残基的点突变通过Gα消除了反应动力学上的差异。这一结果表明，螺旋8的N端酸性残基是通过Gα(15)_(Olf)快速反应的。(C)2015年欧洲生化学会联合会。爱思唯尔出版，版权所有。
We previously observed highly rapid and robust response of murine olfactory receptor S6 (mOR-S6) with chimeric G alpha(15)_(olf) , compared to G alpha(15). To identify residues responsible for this difference in response, mutations of the cytosolic helix 8 were analyzed in a heterologous functional expression system. The N-terminal hydrophobic core between helix 8 and TM1-2 of mOR-S6 is important for activation of both G alpha(15)_(olf) and G alpha(15). Point mutation of a helix 8 N-terminal acidic residue eliminated the differences in response dynamics via G alpha. This result suggests that an N-terminal acidic residue of helix 8 is responsible for rapid response via G alpha(15)_(olf). (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.