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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...

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Detalles Bibliográficos
Autores principales: Yue, Jingyin, Huhn, Steven, Shen, Zhiyuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
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.
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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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