STIM Proteins: An Ever-Expanding Family.

STIM Proteins: An Ever-Expanding Family.
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DOI:
10.3390/ijms22010378
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发表时间:
2020-12-31
影响因子:
5.6
通讯作者:
Fahrner M
Fahrner M
中科院分区:
生物学2区
文献类型:
--
作者:
Grabmayr H;Romanin C;Fahrner M

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基质相互作用分子(STIM)是一类独特的在内质网(ER)膜上普遍表达的单代跨膜蛋白。它们与质膜(PM)中的Orai离子通道一起构成钙释放活化钙(CRAC)通道的分子基础。一种被称为储存操作钙进入(SOCE)的细胞内信号通路严重依赖于CRAC通道。SOCE途径被配体诱导的内质网钙储存耗尽激活。STIM蛋白作为钙传感器,随后感知这种耗尽并通过直接物理相互作用激活Orai离子通道,从而允许钙离子流入进行储存再填充和下游信号传导过程。本文综述了STIM蛋白研究领域的最新进展。基于最近发表的功能数据以及核磁共振(NMR)光谱和分子动力学(MD)模拟的结构数据,报告了正在进行的研究的新结果,并讨论了STIM蛋白亚型及其在调节SOCE中的差异功能的最新研究进展。
Stromal interaction molecules (STIM) are a distinct class of ubiquitously expressed single-pass transmembrane proteins in the endoplasmic reticulum (ER) membrane. Together with Orai ion channels in the plasma membrane (PM), they form the molecular basis of the calcium release-activated calcium (CRAC) channel. An intracellular signaling pathway known as store-operated calcium entry (SOCE) is critically dependent on the CRAC channel. The SOCE pathway is activated by the ligand-induced depletion of the ER calcium store. STIM proteins, acting as calcium sensors, subsequently sense this depletion and activate Orai ion channels via direct physical interaction to allow the influx of calcium ions for store refilling and downstream signaling processes. This review article is dedicated to the latest advances in the field of STIM proteins. New results of ongoing investigations based on the recently published functional data as well as structural data from nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations are reported and complemented with a discussion of the latest developments in the research of STIM protein isoforms and their differential functions in regulating SOCE.
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期刊: STORE-OPERATED CA2+ ENTRY (SOCE) PATHWAYS: EMERGING SIGNALING CONCEPTS IN HUMAN (PATHO)PHYSIOLOGY, 2ND EDITION
影响因子: --
作者:
Fahrner, Marc;Schindl, Rainer;Romanin, Christoph
通讯作者: Romanin, Christoph