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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Targeted expression of the inositol 1,4,5-triphosphate receptor (IP_3R) ligand-binding domain releases Ca~(2+) via endogenous IP_3R channels
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Targeted expression of the inositol 1,4,5-triphosphate receptor (IP_3R) ligand-binding domain releases Ca~(2+) via endogenous IP_3R channels

机译：肌醇1,4,5-三磷酸受体（IP_3R）配体结合域的靶向表达通过内源IP_3R通道释放Ca〜（2+）

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摘要

Virtually all functions of a cell are influenced by cytoplasmic [Ca~(2+)] increases. Inositol 1,4,5-trisphosphate receptor (IP_3R) channels, located in the endoplasmic reticulum (ER), release Ca~(2+) in response to binding of the second messenger, IP_3. IP_3Rs thus are part of the information chain interpreting external signals and transforming them into cytoplasmic Ca~(2+) transients. IP_3Rs function as tetramers, each unit comprising an N-terminal ligand-binding domain (LBD) and a C-terminal channel domain linked by a long regulatory region. It is not yet understood how the binding of IP_3 to the LBD regulates the gating properties of the channel. Here, we use the expression of IP_3 binding protein domains tethered to the surface of the endoplasmic reticulum (ER) to show that the all-helical domain of the IP_3R LBD is capable of depleting the ER Ca~(2+) pools by opening the endogenous IP_3Rs, even without IP_3 binding. This effect requires the domain to be within 50 A of the ER membrane and is impaired by the presence of the N-terminal inhibitory segment on the LBD. These findings raise the possibility that the helical domain of the LBD functions as an effector module possibly interacting with the channei domain, therebv being part of the gating mechanisms by which the IP_3-induced conformational change within the LBD regulates Ca~(2+) release.
机译：实际上，细胞的所有功能都受细胞质[Ca〜（2+）]增加的影响。位于内质网（ER）的肌醇1,4,5-三磷酸受体（IP_3R）通道响应第二信使IP_3的结合释放Ca〜（2+）。 IP_3R因此是信息链的一部分，解释外部信号并将其转换为胞质Ca〜（2+）瞬变。 IP_3R充当四聚体，每个单元包含一个N端配体结合结构域（LBD）和一个C端通道结构域，该结构域通过长调控区连接。尚不了解IP_3与LBD的绑定如何调节通道的门控特性。在这里，我们使用束缚于内质网（ER）表面的IP_3结合蛋白结构域的表达来显示IP_3R LBD的全螺旋结构域能够通过打开内质网来消耗ER Ca〜（2+）库。内源IP_3R，即使没有IP_3绑定也是如此。该作用要求该结构域在ER膜的50 A以内，并且由于LBD上N端抑制性区段的存在而受损。这些发现增加了LBD的螺旋结构域充当可能与通道结构域相互作用的效应子模块的可能性，这是门控机制的一部分，通过该门控机制，LBD中的IP_3诱导的构象变化调节Ca〜（2+）释放。 。

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