The N-terminal domain of the IP3 receptor gates store-operated hTrp3 channels
The N-terminal domain of the IP3 receptor gates store-operated hTrp3 channels
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DOI：
10.1016/s1097-2765(00)80344-5
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发表时间：
1999-09-01
期刊：
影响因子：
16
通讯作者：
Muallem, S
中科院分区：
文献类型：
--
作者：
Kiselyov, K;Mignery, GA;Muallem, S
在目前的工作中，我们研究了几种IP 3受体（IP 3R）结构对商店操作（SOC）的hTrp 3通道的门控的相互作用和效果。全长IP 3R耦合到沉默的hTrp 3通道在完整的细胞，但不激活它们，直到商店耗尽的Ca 2+。相比之下，含有IP 3结合结构域的构建体在未刺激的细胞中激活沉默的hTrp 3通道，并在切除的质膜贴片中通过IP 3恢复hTrp 3的门控。我们得出结论，IP 3R的N-末端结构域的功能作为一个门，是足以激活SOC。IP 3R的传感和转导结构域是维持SOC处于非活性状态所必需的。
In the present work, we studied the interaction and effect of several IP3 receptor (IP3R) constructs on the gating of the store-operated (SOC) hTrp3 channel. Full-length IP3R coupled to silent hTrp3 channels in intact cells but did not activate them until stores were depleted of Ca2+. By contrast, constructs containing the IP3-binding domain activated silent hTrp3 channels in unstimulated cells and restored gating of hTrp3 by IP3 in excised plasma membrane patches. We conclude that the N-terminal domain of the IP3R functions as a gate and is sufficient for activation of SOCs. The sensing and transduction domains of the IP3R are required to maintain SOCs in an inactive state.