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Protein family review

The ADF/cofilin family: actin-remodeling proteins

Sutherland K Maciver1* and Patrick J Hussey2

Author Affiliations

1 Genes and Development Interdisciplinary Group, Department of Biomedical Sciences, University of Edinburgh, George Square, Edinburgh EH8 9XD, Scotland, UK

2 The Intergrative Biology Laboratory, School of Biological Sciences, University of Durham, South Road, Durham DH1 3LE, UK

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Genome Biology 2002, 3:reviews3007-reviews3007.12  doi:10.1186/gb-2002-3-5-reviews3007

Published: 26 April 2002

Abstract

The ADF/cofilins are a family of actin-binding proteins expressed in all eukaryotic cells so far examined. Members of this family remodel the actin cytoskeleton, for example during cytokinesis, when the actin-rich contractile ring shrinks as it contracts through the interaction of ADF/cofilins with both monomeric and filamentous actin. The depolymerizing activity is twofold: ADF/cofilins sever actin filaments and also increase the rate at which monomers leave the filament's pointed end. The three-dimensional structure of ADF/cofilins is similar to a fold in members of the gelsolin family of actin-binding proteins in which this fold is typically repeated three or six times; although both families bind polyphosphoinositide lipids and actin in a pH-dependent manner, they share no obvious sequence similarity. Plants and animals have multiple ADF/cofilin genes, belonging in vertebrates to two types, ADF and cofilins. Other eukaryotes (such as yeast, Acanthamoeba and slime moulds) have a single ADF/cofilin gene. Phylogenetic analysis of the ADF/cofilins reveals that, with few exceptions, their relationships reflect conventional views of the relationships between the major groups of organisms.