与STIM1和储存操作Ca2+进入相互作用的蛋白质。

Wen-An Wang, Nicolas Demaurex
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引用次数: 3

摘要

内质网(ER) Ca2+传感器基质相互作用分子1 (STIM1)与质膜上的ORAI Ca2+通道相互作用,调节免疫和肌肉细胞功能。STIM1激活、易位、ORAI1捕获和门控背后的构象变化受到翻译后修饰和辅助蛋白的严格调控。在这里,我们回顾了最近在鉴定和表征内质网和细胞质蛋白与STIM1相互作用以控制其在储存操作的Ca2+进入(SOCE)过程中的激活和失活的进展。
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Proteins Interacting with STIM1 and Store-Operated Ca2+ Entry.

The endoplasmic reticulum (ER) Ca2+ sensor stromal interaction molecule 1 (STIM1) interacts with ORAI Ca2+ channels at the plasma membrane to regulate immune and muscle cell function. The conformational changes underlying STIM1 activation, translocation, and ORAI1 trapping and gating, are stringently regulated by post-translational modifications and accessory proteins. Here, we review the recent progress in the identification and characterization of ER and cytosolic proteins interacting with STIM1 to control its activation and deactivation during store-operated Ca2+ entry (SOCE).

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来源期刊
CiteScore
3.30
自引率
0.00%
发文量
7
期刊介绍: Molecular biology has been providing an overwhelming amount of data on the structural components and molecular machineries of the cell and its organelles and the complexity of intra- and intercellular communication. The molecular basis of hereditary and acquired diseases is beginning to be unravelled, and profound new insights into development and evolutionary biology have been gained from molecular approaches. Progress in Molecular and Subcellular Biology summarises the most recent developments in this fascinating area of biology.
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