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The ADF/cofilin family: actin-remodeling proteins

Author:
Maciver, Sutherland K, Hussey, Patrick J
Source:
Genome biology 2002 v.3 no.5 pp. 365
ISSN:
1474-760X
Subject:
Acanthamoeba, actin, cytokinesis, eukaryotic cells, genes, lipids, microfilaments, pH, phylogeny, plants (botany), protein synthesis, sequence homology, vertebrates, yeasts
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.
Agid:
1194690