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Twinfilin, a molecular mailman for actin monomers

Program in Cellular Biotechnology, Institute of Biotechnology, PO Box 56, 00014 University of Helsinki, Finland

^* Author for correspondence (e-mail: pekka.lappalainen{at}helsinki.fi )

Twinfilin is a ubiquitous actin-monomer-binding protein that is composed of two ADF-homology domains. It forms a 1:1 complex with ADP-actin-monomers, inhibits nucleotide exchange on actin monomers and prevents assembly of the monomer into filaments. The two ADF-H domains in twinfilin probably have 3D structures similar to those of the ADF/cofilin proteins and overlapping actin-binding sites. Twinfilin also interacts with PtdIns(4,5)P₂, which inhibits its actin-monomer-sequestering activity in vitro. Mutations in the twinfilin gene result in defects in the bipolar budding pattern in S. cerevisiae and in a rough eye phenotype and aberrant bristle morphology in Drosophila melanogaster. These phenotypes are caused by the uncontrolled polymerization of actin filaments in the absence of twinfilin. Studies on budding yeast suggest that twinfilin contributes to actin filament turnover by localizing actin monomers, in their `inactive' ADP-form, to the sites of rapid filament assembly. This is mediated through direct interactions between twinfilin and capping protein. Therefore, twinfilin might serve as a link between rapid actin filament depolymerization and assembly in cells.

Key words: Actin, Twinfilin, ADF-H domain, Capping protein, Cytoskeletal dynamics

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