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

      review-article
      Author(s): 1 , 2 , 1 , 1 ,
      Publication date (Electronic):
      Journal: Cell & Bioscience
      Publisher: BioMed Central
      Keywords: Filamin-A, ABP-280, Actin filament, Cytoskeleton, DNA repair, Metastasis

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          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.

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          Filamins as integrators of cell mechanics and signalling.

          T Stossel, J Condeelis, L. Cooley … (2001)
          Filamins are large actin-binding proteins that stabilize delicate three-dimensional actin webs and link them to cellular membranes. They integrate cellular architectural and signalling functions and are essential for fetal development and cell locomotion. Here, we describe the history, structure and function of this group of proteins.
          Article 0 comments Cited 227 times – based on 0 reviews     Review now
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            Defining molecular profiles of poor outcome in patients with invasive bladder cancer using oligonucleotide microarrays.

            Marta Sánchez-Carbayo, Nicholas D. Socci, Juanjo Lozano … (2006)
            Bladder cancer is a common malignancy characterized by a poor clinical outcome when tumors progress into invasive disease. We sought to define genetic signatures characteristic of aggressive clinical behavior in advanced bladder tumors. Oligonucleotide arrays were utilized to analyze the transcript profiles of 105 bladder tumors: 33 superficial, 72 invasive lesions, and 52 normal urothelium. Hierarchical clustering and supervised algorithms were used to classify and stratify bladder tumors on the basis of stage, node metastases, and overall survival. Immunohistochemical analyses on bladder cancer tissue arrays (n = 294 cases) served to validate associations between marker expression, staging and outcome. Hierarchical clustering classified normal urothelium, superficial, and invasive tumors with 82.2% accuracy, and stratified bladder tumors on the basis of clinical outcome. Predictive algorithms rendered an 89%-correct rate for tumor staging using genes differentially expressed between superficial and invasive tumors. Accuracies of 82% and 90% were obtained for predicting overall survival when considering all patients with bladder cancer or only patients with invasive disease, respectively. A genetic profile consisting of 174 probes was identified in those patients with positive lymph nodes and poor survival. Two independent Global Test runs confirmed the robust association of this profile with lymph node metastases (P = 7.3(-13)) and overall survival (P = 1.9(-14)) simultaneously. Immunohistochemical analyses on tissue arrays sustained the significant association of synuclein with tumor staging and clinical outcome (P = .002). Gene profiling provides a genomic-based classification scheme of diagnostic and prognostic utility for stratifying advanced bladder cancer. Identification of this poor outcome profile could assist in selecting patients who may benefit from more aggressive therapeutic intervention.
            Article 0 comments Cited 170 times – based on 0 reviews     Review now
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              Mutations in filamin 1 prevent migration of cerebral cortical neurons in human periventricular heterotopia.

              J W Fox, E D Lamperti, Y Z Ekşioğlu … (1998)
              Long-range, directed migration is particularly dramatic in the cerebral cortex, where postmitotic neurons generated deep in the brain migrate to form layers with distinct form and function. In the X-linked dominant human disorder periventricular heterotopia (PH), many neurons fail to migrate and persist as nodules lining the ventricular surface. Females with PH present with epilepsy and other signs, including patent ductus arteriosus and coagulopathy, while hemizygous males die embryonically. We have identified the PH gene as filamin 1 (FLN1), which encodes an actin-cross-linking phosphoprotein that transduces ligand-receptor binding into actin reorganization, and which is required for locomotion of many cell types. FLN1 shows previously unrecognized, high-level expression in the developing cortex, is required for neuronal migration to the cortex, and is essential for embryogenesis.
              Article 0 comments Cited 135 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Jingyin Yue
                Steven Huhn
                Zhiyuan Shen
                Journal
                Journal ID (nlm-ta): Cell Biosci
                Journal ID (iso-abbrev): Cell Biosci
                Title: Cell & Bioscience
                Publisher: BioMed Central
                ISSN (Electronic): 2045-3701
                Publication date Collection: 2013
                Publication date (Electronic): 6 February 2013
                Volume: 3
                Page: 7
                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
                Article
                Publisher ID: 2045-3701-3-7
                DOI: 10.1186/2045-3701-3-7
                PMC ID: 3573937
                PubMed ID: 23388158
                SO-VID: 4fc80c17-12b0-4705-812b-a8f0b9349d29
                Copyright © Copyright ©2013 Yue et al.; licensee BioMed Central Ltd.
                License:

                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.

                History
                Date received : 27 December 2012
                Date accepted : 10 January 2013
                Categories
                Subject: Review

                ScienceOpen disciplines: Cell biology
                Keywords: filamin-a,abp-280,actin filament,cytoskeleton,dna repair,metastasis
                Data availability:
                ScienceOpen disciplines: Cell biology
                Keywords: filamin-a, abp-280, actin filament, cytoskeleton, dna repair, metastasis

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