Senju Yosuke, Tsai Feng-Ching
Research Institute for Interdisciplinary Science (RIIS), Okayama University, Okayama, Japan.
Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico Chimie Curie, 75005 Paris, France.
Biophys Rev. 2022 Jan 28;14(1):199-208. doi: 10.1007/s12551-021-00928-0. eCollection 2022 Feb.
Many signal transductions resulting from ligand-receptor interactions occur at the cell surface. These signaling pathways play essential roles in cell polarization, membrane morphogenesis, and the modulation of membrane tension at the cell surface. However, due to the large number of membrane-binding proteins, including actin-membrane linkers, and transmembrane proteins present at the cell surface, the molecular mechanisms underlying the regulation at the cell surface are yet unclear. Here, we describe the molecular functions of one of the key players at the cell surface, ezrin/radixin/moesin (ERM) proteins from a biophysical point of view. We focus our discussion on biophysical properties of ERM proteins revealed by using biophysical tools in live cells and in vitro reconstitution systems. We first describe the structural properties of ERM proteins and then discuss the interactions of ERM proteins with PI(4,5)P and the actin cytoskeleton. These properties of ERM proteins revealed by using biophysical approaches have led to a better understanding of their physiological functions in cells and tissues.
The online version contains supplementary material available at 10.1007/s12551-021-00928-0.
许多由配体-受体相互作用产生的信号转导发生在细胞表面。这些信号通路在细胞极化、膜形态发生以及细胞表面膜张力的调节中起着至关重要的作用。然而，由于细胞表面存在大量的膜结合蛋白，包括肌动蛋白-膜连接蛋白和跨膜蛋白，细胞表面调节的分子机制仍不清楚。在这里，我们从生物物理学的角度描述细胞表面关键蛋白之一埃兹蛋白/根蛋白/膜突蛋白（ERM）的分子功能。我们将讨论重点放在通过在活细胞和体外重组系统中使用生物物理工具揭示的ERM蛋白的生物物理特性上。我们首先描述ERM蛋白的结构特性，然后讨论ERM蛋白与PI(4,5)P和肌动蛋白细胞骨架的相互作用。通过生物物理方法揭示的ERM蛋白的这些特性，使我们对其在细胞和组织中的生理功能有了更好的理解。
在线版本包含可在10.1007/s12551-021-00928-0获取的补充材料。
