Receptor guanylyl cyclase-G is a novel thermosensory protein activated by cool temperatures
Receptor guanylyl cyclase-G is a novel thermosensory protein activated by cool temperatures
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DOI：
10.15252/embj.201489652
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发表时间：
2015-02-03
期刊：
影响因子：
11.4
通讯作者：
Yang, Ruey-Bing
中科院分区：
文献类型：
--
作者：
Chao, Ying-Chi;Chen, Chih-Cheng;Yang, Ruey-Bing
跨膜鸟苷酸环化酶（GCs），其活性受肽配体和/或钙结合蛋白的调节，是各种生理和感觉过程所必需的。GC亚型GC-G的激活模式一直难以捉摸，该亚型在对低温有反应的Grueneberg神经节的神经元中表达。在寻找合适的刺激来激活GC-G，我们发现它的酶活性直接刺激低温。在这种情况下，观察到GC-G的二聚/寡聚（通常认为对GC的酶活性至关重要的过程）通过冷却强烈增强。此外，在培养细胞中异源表达GC-G使这些细胞对凉爽有反应;因此，该蛋白可能是凉爽温度的传感器。这一概念得到了支持的观察显着减少凉爽引起的反应Grueneberg神经节神经元和凉爽诱发的超声波发声GC-G缺陷的小鼠幼崽。GC-G可能是一种新型的热敏蛋白，其功能与Grueneberg神经节有关，Grueneberg神经节是一种对低温做出反应的感觉器官。
Transmembrane guanylyl cyclases (GCs), with activity regulated by peptide ligands and/or calcium-binding proteins, are essential for various physiological and sensory processes. The mode of activation of the GC subtype GC-G, which is expressed in neurons of the Grueneberg ganglion that respond to cool temperatures, has been elusive. In searching for appropriate stimuli to activate GC-G, we found that its enzymatic activity is directly stimulated by cool temperatures. In this context, it was observed that dimerization/oligomerization of GC-G, a process generally considered as critical for enzymatic activity of GCs, is strongly enhanced by coolness. Moreover, heterologous expression of GC-G in cultured cells rendered these cells responsive to coolness; thus, the protein might be a sensor for cool temperatures. This concept is supported by the observation of substantially reduced coolness-induced response of Grueneberg ganglion neurons and coolness-evoked ultrasonic vocalization in GC-G-deficient mouse pups. GC-G may be a novel thermosensory protein with functional implications for the Grueneberg ganglion, a sensory organ responding to cool temperatures.