C. elegans TRP family protein TRP-4 is a pore-forming subunit of a native mechanotransduction channel.
C. elegans TRP family protein TRP-4 is a pore-forming subunit of a native mechanotransduction channel.
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线虫 TRP 家族蛋白 TRP-4 是天然机械转导通道的成孔亚基
DOI：
10.1016/j.neuron.2010.06.032
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发表时间：
2010-08-12
期刊：
影响因子：
16.2
通讯作者：
Xu XZ
中科院分区：
文献类型：
--
作者：
Kang L;Gao J;Schafer WR;Xie Z;Xu XZ
机械传导通道介导几种常见的感觉方式，如听觉，触觉和本体感受;然而，对这些通道的分子身份知之甚少。许多TRP家族通道与机械感觉有关，但没有一个被证明能形成机械转导通道，这就提出了TRP蛋白是否只是在机械感觉中起间接作用的问题。利用C. elegans作为模型，在这里，我们记录了在体内纤毛机械感觉神经元的机械敏感电导。这种电导在机械刺激时发展非常迅速，其潜伏期和激活时间常数达到微秒范围，与电导的机械门控一致。TRP-4，一个TRPN（NOMPC）亚家族通道，是这种电导所必需的。重要的是，TRP-4的预测孔区域中的点突变改变了电导的离子选择性。这些结果确定TRP-4作为第一个TRP蛋白，作为一个必要的孔形成亚基的天然机械转导通道的功能。
Mechanotransduction channels mediate several common sensory modalities such as hearing, touch, and proprioception; however, very little is known about the molecular identities of these channels. Many TRP family channels have been implicated in mechanosensation, but none of them has been demonstrated to form a mechanotransduction channel, raising the question of whether TRP proteins simply play indirect roles in mechanosensation. Using C. elegans as a model, here we have recorded a mechanosensitive conductance in a ciliated mechanosensory neuron in vivo. This conductance develops very rapidly upon mechanical stimulation with its latency and activation time constant reaching the range of micro-seconds, consistent with mechanical gating of the conductance. TRP-4, a TRPN (NOMPC) subfamily channel, is required for this conductance. Importantly, point mutations in the predicted pore region of TRP-4 alter the ion selectivity of the conductance. These results identify TRP-4 as the first TRP protein that functions as an essential pore-forming subunit of a native mechanotransduction channel.
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