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Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin

Ezrin is one of the members of the ezrin/radixin/moesin (ERM) family of proteins. It was originally discovered as an actin-binding protein in the microvilli structure about forty years ago. Since then, it has been revealed as a key protein with functions in a variety of fields including cell migrati...

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Autores principales: Kawaguchi, Kotoku, Asano, Shinji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8952289/
https://www.ncbi.nlm.nih.gov/pubmed/35328667
http://dx.doi.org/10.3390/ijms23063246
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author Kawaguchi, Kotoku
Asano, Shinji
author_facet Kawaguchi, Kotoku
Asano, Shinji
author_sort Kawaguchi, Kotoku
collection PubMed
description Ezrin is one of the members of the ezrin/radixin/moesin (ERM) family of proteins. It was originally discovered as an actin-binding protein in the microvilli structure about forty years ago. Since then, it has been revealed as a key protein with functions in a variety of fields including cell migration, survival, and signal transduction, as well as functioning as a structural component. Ezrin acts as a cross-linker of membrane proteins or phospholipids in the plasma membrane and the actin cytoskeleton. It also functions as a platform for signaling molecules at the cell surface. Moreover, ezrin is regarded as an important target protein in cancer diagnosis and therapy because it is a key protein involved in cancer progression and metastasis, and its high expression is linked to poor survival in many cancers. Small molecule inhibitors of ezrin have been developed and investigated as candidate molecules that suppress cancer metastasis. Here, we wish to comprehensively review the roles of ezrin from the pathophysiological points of view.
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spelling pubmed-89522892022-03-26 Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin Kawaguchi, Kotoku Asano, Shinji Int J Mol Sci Review Ezrin is one of the members of the ezrin/radixin/moesin (ERM) family of proteins. It was originally discovered as an actin-binding protein in the microvilli structure about forty years ago. Since then, it has been revealed as a key protein with functions in a variety of fields including cell migration, survival, and signal transduction, as well as functioning as a structural component. Ezrin acts as a cross-linker of membrane proteins or phospholipids in the plasma membrane and the actin cytoskeleton. It also functions as a platform for signaling molecules at the cell surface. Moreover, ezrin is regarded as an important target protein in cancer diagnosis and therapy because it is a key protein involved in cancer progression and metastasis, and its high expression is linked to poor survival in many cancers. Small molecule inhibitors of ezrin have been developed and investigated as candidate molecules that suppress cancer metastasis. Here, we wish to comprehensively review the roles of ezrin from the pathophysiological points of view. MDPI 2022-03-17 /pmc/articles/PMC8952289/ /pubmed/35328667 http://dx.doi.org/10.3390/ijms23063246 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kawaguchi, Kotoku
Asano, Shinji
Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin
title Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin
title_full Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin
title_fullStr Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin
title_full_unstemmed Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin
title_short Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin
title_sort pathophysiological roles of actin-binding scaffold protein, ezrin
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8952289/
https://www.ncbi.nlm.nih.gov/pubmed/35328667
http://dx.doi.org/10.3390/ijms23063246
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