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Open Access Review

Complex roles of filamin-A mediated cytoskeleton network in cancer progression

Jingyin Yue12, Steven Huhn1 and Zhiyuan Shen1*

Author Affiliations

1 Department of Radiation Oncology, The Cancer Institute of New Jersey, Robert Wood Johnson Medical School, New Brunswick, NJ, 08903, USA

2 Current address: Molecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, New York, NY, 10065, USA

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Cell & Bioscience 2013, 3:7  doi:10.1186/2045-3701-3-7

Published: 6 February 2013

Abstract

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.

Keywords:
Filamin-A; ABP-280; Actin filament; Cytoskeleton; DNA repair; Metastasis