揭示 S100A1 在调节 RyR1 活性中的复杂作用:关于 "S100A1调控RyR1的结构见解 "的评论文章

IF 4.3 2区 生物学 Q2 CELL BIOLOGY Cell calcium Pub Date : 2024-08-23 DOI:10.1016/j.ceca.2024.102947
Megan L. Perry , Kristen M. Varney , Pratyush Tiwary , David J. Weber , Erick O. Hernández-Ochoa
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引用次数: 0

摘要

S100A1 是一种钙结合蛋白,通过与雷诺丁受体(RyR)相互作用,在调节骨骼肌和心肌细胞的 Ca2+ 信号通路中发挥着重要作用,从而影响 Ca2+ 释放和收缩性能。生物物理研究强烈表明,S100A1 与 RyRs 有相互作用,但这种相互作用的性质及其与另一种重要的钙结合蛋白钙调蛋白(CaM)的竞争关系尚无定论。因此,需要对存在 S100A1(无论是否存在额外的 CaM)的 RyRs 进行高分辨率冷冻电镜研究。Weninger 等人的出色研究通过各种实验证明了 S100A1 与 RyR1 之间的相互作用,并证实 S100A1 在亚微摩 Ca2+ 浓度下可激活 RyR1,从而提高 RyR1 通道的开放概率。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Unveiling the intricate role of S100A1 in regulating RyR1 activity: A commentary on “Structural insights into the regulation of RyR1 by S100A1”

S100A1, a calcium-binding protein, plays a crucial role in regulating Ca2+ signaling pathways in skeletal and cardiac myocytes via interactions with the ryanodine receptor (RyR) to affect Ca2+ release and contractile performance. Biophysical studies strongly suggest that S100A1 interacts with RyRs but have been inconclusive about both the nature of this interaction and its competition with another important calcium-binding protein, calmodulin (CaM). Thus, high-resolution cryo-EM studies of RyRs in the presence of S100A1, with or without additional CaM, were needed. The elegant work by Weninger et al. demonstrates the interaction between S100A1 and RyR1 through various experiments and confirms that S100A1 activates RyR1 at sub-micromolar Ca2+ concentrations, increasing the open probability of RyR1 channels.

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来源期刊
Cell calcium
Cell calcium 生物-细胞生物学
CiteScore
8.70
自引率
5.00%
发文量
115
审稿时长
35 days
期刊介绍: Cell Calcium covers the field of calcium metabolism and signalling in living systems, from aspects including inorganic chemistry, physiology, molecular biology and pathology. Topic themes include: Roles of calcium in regulating cellular events such as apoptosis, necrosis and organelle remodelling Influence of calcium regulation in affecting health and disease outcomes
期刊最新文献
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