Review

Cell & Bioscience

, 3:7

Open Access This content is freely available online to anyone, anywhere at any time.

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

  • Jingyin YueAffiliated withDepartment of Radiation Oncology, The Cancer Institute of New Jersey, Robert Wood Johnson Medical SchoolMolecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center
  • , Steven HuhnAffiliated withDepartment of Radiation Oncology, The Cancer Institute of New Jersey, Robert Wood Johnson Medical School
  • , Zhiyuan ShenAffiliated withDepartment of Radiation Oncology, The Cancer Institute of New Jersey, Robert Wood Johnson Medical School Email author 

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