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Complex roles of filamin-A mediated cytoskeleton network in cancer progression
Filamin-A (FLNA), also called actin-binding protein 280 (ABP-280), was originally identified as a non-muscle actin binding protein, which organizes filamentous actin into orthogonal networks and stress fibers. Filamin-A also anchors various transmembrane proteins to the actin cytoskeleton and provid...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3573937/ https://www.ncbi.nlm.nih.gov/pubmed/23388158 http://dx.doi.org/10.1186/2045-3701-3-7 |
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author | Yue, Jingyin Huhn, Steven Shen, Zhiyuan |
author_facet | Yue, Jingyin Huhn, Steven Shen, Zhiyuan |
author_sort | Yue, Jingyin |
collection | PubMed |
description | Filamin-A (FLNA), also called actin-binding protein 280 (ABP-280), was originally identified as a non-muscle actin binding protein, which organizes filamentous actin into orthogonal networks and stress fibers. Filamin-A also anchors various transmembrane proteins to the actin cytoskeleton and provides a scaffold for a wide range of cytoplasmic and nuclear signaling proteins. Intriguingly, several studies have revealed that filamin-A associates with multiple non-cytoskeletal proteins of diverse function and is involved in several unrelated pathways. Mutations and aberrant expression of filamin-A have been reported in human genetic diseases and several types of cancer. In this review, we discuss the implications of filamin-A in cancer progression, including metastasis and DNA damage response. |
format | Online Article Text |
id | pubmed-3573937 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-35739372013-02-16 Complex roles of filamin-A mediated cytoskeleton network in cancer progression Yue, Jingyin Huhn, Steven Shen, Zhiyuan Cell Biosci Review Filamin-A (FLNA), also called actin-binding protein 280 (ABP-280), was originally identified as a non-muscle actin binding protein, which organizes filamentous actin into orthogonal networks and stress fibers. Filamin-A also anchors various transmembrane proteins to the actin cytoskeleton and provides a scaffold for a wide range of cytoplasmic and nuclear signaling proteins. Intriguingly, several studies have revealed that filamin-A associates with multiple non-cytoskeletal proteins of diverse function and is involved in several unrelated pathways. Mutations and aberrant expression of filamin-A have been reported in human genetic diseases and several types of cancer. In this review, we discuss the implications of filamin-A in cancer progression, including metastasis and DNA damage response. BioMed Central 2013-02-06 /pmc/articles/PMC3573937/ /pubmed/23388158 http://dx.doi.org/10.1186/2045-3701-3-7 Text en Copyright ©2013 Yue et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Yue, Jingyin Huhn, Steven Shen, Zhiyuan Complex roles of filamin-A mediated cytoskeleton network in cancer progression |
title | Complex roles of filamin-A mediated cytoskeleton network in cancer progression |
title_full | Complex roles of filamin-A mediated cytoskeleton network in cancer progression |
title_fullStr | Complex roles of filamin-A mediated cytoskeleton network in cancer progression |
title_full_unstemmed | Complex roles of filamin-A mediated cytoskeleton network in cancer progression |
title_short | Complex roles of filamin-A mediated cytoskeleton network in cancer progression |
title_sort | complex roles of filamin-a mediated cytoskeleton network in cancer progression |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3573937/ https://www.ncbi.nlm.nih.gov/pubmed/23388158 http://dx.doi.org/10.1186/2045-3701-3-7 |
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