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Turnover of Focal Adhesions and Cancer Cell Migration
Cells are usually surrounded by the extracellular matrix (ECM), and adhesion of the cells to the ECM is a key step in their migration through tissues. Integrins are important receptors for the ECM and form structures called focal adhesions (FAs). Formation and disassembly of FAs are regulated dynami...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3272802/ https://www.ncbi.nlm.nih.gov/pubmed/22319531 http://dx.doi.org/10.1155/2012/310616 |
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author | Nagano, Makoto Hoshino, Daisuke Koshikawa, Naohiko Akizawa, Toshifumi Seiki, Motoharu |
author_facet | Nagano, Makoto Hoshino, Daisuke Koshikawa, Naohiko Akizawa, Toshifumi Seiki, Motoharu |
author_sort | Nagano, Makoto |
collection | PubMed |
description | Cells are usually surrounded by the extracellular matrix (ECM), and adhesion of the cells to the ECM is a key step in their migration through tissues. Integrins are important receptors for the ECM and form structures called focal adhesions (FAs). Formation and disassembly of FAs are regulated dynamically during cell migration. Adhesion to the ECM has been studied mainly using cells cultured on an ECM-coated substratum, where the rate of cell migration is determined by the turnover of FAs. However, the molecular events underlying the disassembly of FAs are less well understood. We have recently identified both a new regulator of this disassembly process and its interaction partners. Here, we summarize our understanding of FA disassembly by focusing on the proteins implicated in this process. |
format | Online Article Text |
id | pubmed-3272802 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-32728022012-02-08 Turnover of Focal Adhesions and Cancer Cell Migration Nagano, Makoto Hoshino, Daisuke Koshikawa, Naohiko Akizawa, Toshifumi Seiki, Motoharu Int J Cell Biol Review Article Cells are usually surrounded by the extracellular matrix (ECM), and adhesion of the cells to the ECM is a key step in their migration through tissues. Integrins are important receptors for the ECM and form structures called focal adhesions (FAs). Formation and disassembly of FAs are regulated dynamically during cell migration. Adhesion to the ECM has been studied mainly using cells cultured on an ECM-coated substratum, where the rate of cell migration is determined by the turnover of FAs. However, the molecular events underlying the disassembly of FAs are less well understood. We have recently identified both a new regulator of this disassembly process and its interaction partners. Here, we summarize our understanding of FA disassembly by focusing on the proteins implicated in this process. Hindawi Publishing Corporation 2012 2012-01-26 /pmc/articles/PMC3272802/ /pubmed/22319531 http://dx.doi.org/10.1155/2012/310616 Text en Copyright © 2012 Makoto Nagano et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Nagano, Makoto Hoshino, Daisuke Koshikawa, Naohiko Akizawa, Toshifumi Seiki, Motoharu Turnover of Focal Adhesions and Cancer Cell Migration |
title | Turnover of Focal Adhesions and Cancer Cell Migration |
title_full | Turnover of Focal Adhesions and Cancer Cell Migration |
title_fullStr | Turnover of Focal Adhesions and Cancer Cell Migration |
title_full_unstemmed | Turnover of Focal Adhesions and Cancer Cell Migration |
title_short | Turnover of Focal Adhesions and Cancer Cell Migration |
title_sort | turnover of focal adhesions and cancer cell migration |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3272802/ https://www.ncbi.nlm.nih.gov/pubmed/22319531 http://dx.doi.org/10.1155/2012/310616 |
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