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Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis
Focal adhesions (FAs) are specialized structures that enable cells to sense their extracellular matrix rigidity and transmit these signals to the interior of the cells, bringing about actin cytoskeleton reorganization, FA maturation, and cell migration. It is known that cells migrate towards regions...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8637444/ https://www.ncbi.nlm.nih.gov/pubmed/34869319 http://dx.doi.org/10.3389/fcell.2021.735298 |
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author | Yip, Ai Kia Zhang, Songjing Chong, Lor Huai Cheruba, Elsie Woon, Jessie Yong Xing Chua, Theng Xuan Goh, Corinna Jie Hui Yang, Haibo Tay, Chor Yong Koh, Cheng-Gee Chiam, Keng-Hwee |
author_facet | Yip, Ai Kia Zhang, Songjing Chong, Lor Huai Cheruba, Elsie Woon, Jessie Yong Xing Chua, Theng Xuan Goh, Corinna Jie Hui Yang, Haibo Tay, Chor Yong Koh, Cheng-Gee Chiam, Keng-Hwee |
author_sort | Yip, Ai Kia |
collection | PubMed |
description | Focal adhesions (FAs) are specialized structures that enable cells to sense their extracellular matrix rigidity and transmit these signals to the interior of the cells, bringing about actin cytoskeleton reorganization, FA maturation, and cell migration. It is known that cells migrate towards regions of higher substrate rigidity, a phenomenon known as durotaxis. However, the underlying molecular mechanism of durotaxis and how different proteins in the FA are involved remain unclear. Zyxin is a component of the FA that has been implicated in connecting the actin cytoskeleton to the FA. We have found that knocking down zyxin impaired NIH3T3 fibroblast’s ability to sense and respond to changes in extracellular matrix in terms of their FA sizes, cell traction stress magnitudes and F-actin organization. Cell migration speed of zyxin knockdown fibroblasts was also independent of the underlying substrate rigidity, unlike wild type fibroblasts which migrated fastest at an intermediate substrate rigidity of 14 kPa. Wild type fibroblasts exhibited durotaxis by migrating toward regions of increasing substrate rigidity on polyacrylamide gels with substrate rigidity gradient, while zyxin knockdown fibroblasts did not exhibit durotaxis. Therefore, we propose zyxin as an essential protein that is required for rigidity sensing and durotaxis through modulating FA sizes, cell traction stress and F-actin organization. |
format | Online Article Text |
id | pubmed-8637444 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-86374442021-12-03 Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis Yip, Ai Kia Zhang, Songjing Chong, Lor Huai Cheruba, Elsie Woon, Jessie Yong Xing Chua, Theng Xuan Goh, Corinna Jie Hui Yang, Haibo Tay, Chor Yong Koh, Cheng-Gee Chiam, Keng-Hwee Front Cell Dev Biol Cell and Developmental Biology Focal adhesions (FAs) are specialized structures that enable cells to sense their extracellular matrix rigidity and transmit these signals to the interior of the cells, bringing about actin cytoskeleton reorganization, FA maturation, and cell migration. It is known that cells migrate towards regions of higher substrate rigidity, a phenomenon known as durotaxis. However, the underlying molecular mechanism of durotaxis and how different proteins in the FA are involved remain unclear. Zyxin is a component of the FA that has been implicated in connecting the actin cytoskeleton to the FA. We have found that knocking down zyxin impaired NIH3T3 fibroblast’s ability to sense and respond to changes in extracellular matrix in terms of their FA sizes, cell traction stress magnitudes and F-actin organization. Cell migration speed of zyxin knockdown fibroblasts was also independent of the underlying substrate rigidity, unlike wild type fibroblasts which migrated fastest at an intermediate substrate rigidity of 14 kPa. Wild type fibroblasts exhibited durotaxis by migrating toward regions of increasing substrate rigidity on polyacrylamide gels with substrate rigidity gradient, while zyxin knockdown fibroblasts did not exhibit durotaxis. Therefore, we propose zyxin as an essential protein that is required for rigidity sensing and durotaxis through modulating FA sizes, cell traction stress and F-actin organization. Frontiers Media S.A. 2021-11-18 /pmc/articles/PMC8637444/ /pubmed/34869319 http://dx.doi.org/10.3389/fcell.2021.735298 Text en Copyright © 2021 Yip, Zhang, Chong, Cheruba, Woon, Chua, Goh, Yang, Tay, Koh and Chiam. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cell and Developmental Biology Yip, Ai Kia Zhang, Songjing Chong, Lor Huai Cheruba, Elsie Woon, Jessie Yong Xing Chua, Theng Xuan Goh, Corinna Jie Hui Yang, Haibo Tay, Chor Yong Koh, Cheng-Gee Chiam, Keng-Hwee Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis |
title | Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis |
title_full | Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis |
title_fullStr | Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis |
title_full_unstemmed | Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis |
title_short | Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis |
title_sort | zyxin is involved in fibroblast rigidity sensing and durotaxis |
topic | Cell and Developmental Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8637444/ https://www.ncbi.nlm.nih.gov/pubmed/34869319 http://dx.doi.org/10.3389/fcell.2021.735298 |
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