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A more recent version of this article appeared on February 1, 2005
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Submitted on July 6, 2004
Accepted on November 3, 2004
Program in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland
Monitoring Editor: Thomas Pollard
ADF/cofilins are small actin-binding proteins found in all eukaryotes. In vitro, ADF/cofilins promote actin dynamics by depolymerizing and severing actin filaments. However, whether ADF/cofilins contribute to actin dynamics in cells by disassembling ‘old’ actin filaments or by promoting actin filament assembly through their severing activity is a matter of controversy. Analysis of mammalian ADF/cofilins is further complicated by the presence of multiple isoforms, which may contribute to actin dynamics by different mechanisms. We show that two isoforms, ADF and cofilin-1, are expressed in mouse NIH 3T3, B16F1, and Neuro 2A cells. Depleting cofilin-1 and/or ADF by siRNA lead to an accumulation of F-actin and to an increase in cell size. Cofilin-1 and ADF appear to play overlapping roles in cells, because the knockdown phenotype of either protein could be rescued by overexpression of the other one. Cofilin-1 and ADF knockdown cells also had defects in cell motility and cytokinesis, and these defects were most pronounced when both ADF and cofilin-1 were depleted. FRAP (fluorescence recovery after photobleaching) analysis and studies with an actin monomer-sequestering drug, Latrunculin-A, demonstrated that these phenotypes arose from diminished actin filament depolymerization rates. These data suggest that mammalian ADF and cofilin-1 promote cytoskeletal dynamics by depolymerizing actin filaments and that this activity is critical for several processes such as cytokinesis and cell motility.
Present address: Cancer Research UK, London Research Institute, Lincoln’s Inn Fields Laboratories, 44 Lincoln’s Inn Fields, London WC2A 3PX, United Kingdom.
*Corresponding author.
E-mail: pirta.hotulainen{at}helsinki.fi
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