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通过扩展的突触胺介导的PI(4,5) P(2) 依存和Ca(2+) 调节的ER-PM相互作用

Francesca Giordano¹, Yasunori Saheki, Olof Idevall-Hagren

¹Department of Cell Biology, Program in Cellular Neuroscience, Neurodegeneration, and Repair, and Howard Hughes Medical Institute, Yale School of Medicine, New Haven, CT 06510, USA.

|June 25, 2013

概括

扩展的合成胺蛋白 (E-Syts) 将内分泌网膜连接到血膜,调节细胞生理学. 这些E-Syt连接器与参与进入的连接器不同.

科学领域:

细胞生物学细胞生物学
分子生物学分子生物学
生物化学生物化学

背景情况:

细胞内网膜 (ER) - 血膜 (PM) 接触对于细胞功能至关重要.
虽然Ca2+) 进入规则得到了充分的研究,但可能存在其他ER-PM tethers.
扩展的合成胺 (E-Syt) 蛋白质无处不在表达,并与ER-PM连接有关.

研究的目的:

调查E-Syts在形成ER-PM联系人中的作用.
确定E-Syt介导联网的分子机制和调节因素.
为了区分E-Syt-依赖的接触者和那些参与存储运行的入口的人.

主要方法:

生物化学测试用于研究蛋白质相互作用.
细胞成像可视化ER-PM的接触点.
基因操纵来评估E-Syts的功能.

主要成果:

通过与PM的C2域互动,E-Syts作为ER-PM连接器起作用.
E-Syt2和E-Syt3需要PI(4,5) P2,而E-Syt1需要高细胞质Ca(2+).
E-Syts形成异构体复合体,赋予接触形成的Ca2+) 调节.
取决于E-Syt的联系是独立于商店运行的Ca2+) 条目.

结论:

电子系统介绍了功能上不同的ER-PM联系站点的形成.
这些依赖E-Syt的接触点在细胞生理学中发挥着普遍的作用,超出了Ca2+) 调节.
以E-Syt为媒介的连接与依赖STIM1/Orai1的机制不同.

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