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Review
. 2013 Mar-Apr;7(2):199-213.
doi: 10.4161/cam.23176. Epub 2013 Jan 9.

Actin binding proteins: their ups and downs in metastatic life

Stephane R Gross  1
Affiliations
Review

Actin binding proteins: their ups and downs in metastatic life

Stephane R Gross. Cell Adh Migr. 2013 Mar-Apr.

Abstract

In order to metastasize away from the primary tumor site and migrate into adjacent tissues, cancer cells will stimulate cellular motility through the regulation of their cytoskeletal structures. Through the coordinated polymerization of actin filaments, these cells will control the geometry of distinct structures, namely lamella, lamellipodia and filopodia, as well as the more recently characterized invadopodia. Because actin binding proteins play fundamental functions in regulating the dynamics of actin polymerization, they have been at the forefront of cancer research. This review focuses on a subset of actin binding proteins involved in the regulation of these cellular structures and protrusions, and presents some general principles summarizing how these proteins may remodel the structure of actin. The main body of this review aims to provide new insights into how the expression of these actin binding proteins is regulated during carcinogenesis and highlights new mechanisms that may be initiated by the metastatic cells to induce aberrant expression of such proteins.

Keywords: Arp2/3; WASP; ZBP1; actin; cancer; fascin; miRNAs; tropomyosin.

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Figures

None
Figure 1. Actin organization in migrating cancer cell. (A) Staining for F-actin using Phalloidin-Alexa488 in a migrating Rama 37 malignant cell expressing high levels of S100A4. In this image, the structures of lamellipodium/lamellum and filopodium are clearly visible at the leading edge of the cell. (B and C) present models for the lamellipodium/lamellum and filopodium and the respective molecular organization within, focusing on the proteins presented in this review. (B) A simplified model for lamellipodium/lamellum formation. In the lamellipodium, free barbed ends of actin filaments recruit the Arp2/3 complex via activation by WASP/WAVE complex and cortactin. The Arp2/3 complex nucleates a new actin filament from the side of existing filaments and remains at the branching point. In the lamellum, actin filaments are bound to tropomyosins, preventing interactions with other actin binding proteins. (C) A simplified model for filopodia formation. Individual filaments of the filopodium emerge from the branching point on other filaments, through actin polymerization promoted by the Arp2/3 complex. Further addition of actin monomers at the barbed end of actin filaments is nucleated by the formin family, whereas fascin regulates filopodia stability through its bundling activities.
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