Calnexin revealed as an ether-a-go-go chaperone by getting mutant worms up and going.

Calnexin revealed as an ether-a-go-go chaperone by getting mutant worms up and going.
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DOI:
10.1085/jgp.201812068
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发表时间:
2018-08-06
期刊:
The Journal of general physiology
影响因子:
--
通讯作者:
Pierce JT
Pierce JT
中科院分区:
其他
文献类型:
--
作者:
Pierce JT

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Pierce研究了新的工作,揭示了钙连接蛋白控制秀丽隐杆线虫ERG型K+通道的生物发生。离子通道在细胞兴奋性中的作用最早是在20世纪50年代由Hodgkin和Huxley进行的一系列电压钳实验中发现的。然而,直到20世纪70年代,膜片钳记录才迎来了一场革命,使生理学家能够见证离子通道如何以埃级和微秒级分辨率闪烁打开和关闭。后来,在全细胞配置中,贴片吸管出乎意料地紧密密封,使分子生物学家能够吸取已识别细胞的内部,以揭示其独特的分子内容。通过改进这些技术,研究人员在过去几十年中详细检查了可兴奋细胞的表面和内容物。然而,这些强大的方法不能辨别哪些分子负责离子通道的发生、丰度和亚细胞定位的动态控制。在这个黑暗的领域,未知和知之甚少的分子团队通过翻译,折叠和修饰来引导特定的离子通道,然后通过不同的亚细胞途径将它们穿梭于不同的膜结构域。理解这些过程的核心挑战是这些不同的调节分子可能对离子通道亚型、细胞类型和环境具有特异性的可能性。在本期描述的工作中,Bai et al.(2018. J. Gen. Physiol. https://doi.org/10.1085/jgp.201812025)开始阐明了在秀丽隐杆线虫中发现的K+通道-
Pierce examines new work revealing that calnexin controls the biogenesis of ERG-type K+ channels in Caenorhabditis elegans. The role of ion channels in cell excitability was first revealed in a series of voltage clamp experiments by Hodgkin and Huxley in the 1950s. However, it was not until the 1970s that patch-clamp recording ushered in a revolution that allowed physiologists to witness how ion channels flicker open and closed at angstrom scale and with microsecond resolution. The unexpectedly tight seal made by the patch pipette in the whole-cell configuration later allowed molecular biologists to suck up the insides of identified cells to unveil their unique molecular contents. By refining these techniques, researchers have scrutinized the surface and contents of excitable cells in detail over the past few decades. However, these powerful approaches do not discern which molecules are responsible for the dynamic control of the genesis, abundance, and subcellular localization of ion channels. In this dark territory, teams of unknown and poorly understood molecules guide specific ion channels through translation, folding, and modification, and then they shuttle them toward and away from distinct membrane domains via different subcellular routes. A central challenge in understanding these processes is the likelihood that these diverse regulatory molecules may be specific to ion channel subtypes, cell types, and circumstance. In work described in this issue, Bai et al. (2018. J. Gen. Physiol. https://doi.org/10.1085/jgp.201812025) begin to shed light on the biogenesis of UNC-103, a K+ channel found in Caenorhabditis elegans.
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