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A biophysical perspective of the regulatory mechanisms of ezrin/radixin/moesin proteins.
Senju, Yosuke; Tsai, Feng-Ching.
Afiliación
  • Senju Y; Research Institute for Interdisciplinary Science (RIIS), Okayama University, Okayama, Japan.
  • Tsai FC; Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico Chimie Curie, 75005 Paris, France.
Biophys Rev ; 14(1): 199-208, 2022 Feb.
Article en En | MEDLINE | ID: mdl-35340609
ABSTRACT
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)P2 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. Supplementary Information The online version contains supplementary material available at 10.1007/s12551-021-00928-0.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biophys Rev Año: 2022 Tipo del documento: Article País de afiliación: Japón

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biophys Rev Año: 2022 Tipo del documento: Article País de afiliación: Japón
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