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Published online July 14, 2008
doi:10.1083/jcb.200803100
The Journal of Cell Biology, Vol. 182, No. 1, 51-59
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Paavilainen et al.
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 Structure of the actin-depolymerizing factor homology domain in complex with actin

Ville O. Paavilainen1, Esko Oksanen2, Adrian Goldman2,3, and Pekka Lappalainen1

1 Program in Cellular Biotechnology and 2 Program in Structural Biology and Biophysics, Institute of Biotechnology, and 3 Neuroscience Center, University of Helsinki, Helsinki FIN-00014, Finland

Correspondence to Pekka Lappalainen: pekka.lappalainen{at}helsinki.fi

Actin dynamics provide the driving force for many cellular processes including motility and endocytosis. Among the central cytoskeletal regulators are actin-depolymerizing factor (ADF)/cofilin, which depolymerizes actin filaments, and twinfilin, which sequesters actin monomers and caps filament barbed ends. Both interact with actin through an ADF homology (ADF-H) domain, which is also found in several other actin-binding proteins. However, in the absence of an atomic structure for the ADF-H domain in complex with actin, the mechanism by which these proteins interact with actin has remained unknown. Here, we present the crystal structure of twinfilin's C-terminal ADF-H domain in complex with an actin monomer. This domain binds between actin subdomains 1 and 3 through an interface that is conserved among ADF-H domain proteins. Based on this structure, we suggest a mechanism by which ADF/cofilin and twinfilin inhibit nucleotide exchange of actin monomers and present a model for how ADF/cofilin induces filament depolymerization by weakening intrafilament interactions.

V.O. Paavilainen's present address is Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158.

Abbreviations used in this paper: ADF-H, actin-depolymerizing factor homology; NBD, 7-chloro-4-nitrobenz-2-oxa-1,3-diazole; WH2, WASP homology 2.


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