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doi: 10.1242/10.1242/jcs.00611


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Journal of Cell Science 116, 2603-2611 (2003)
doi: 10.1242/jcs.00611


Commentary

Formins: signaling effectors for assembly and polarization of actin filaments

Marie Evangelista1, Sally Zigmond2 and Charles Boone1,3,*

1 Department of Biology, Queen's University, Kingston, Ontario, Canada K7L 3N6
2 Biology Department, University of Pennsylvania, Philadelphia, PA 19104-6018, USA
3 Banting and Best Department of Medical Research and Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, Canada M5G 1L6

* Author for correspondnce (e-mail: charlie.boone{at}utoronto.ca)

Eukaryotic cells require filamentous actin to maintain their shape and for movement, growth and replication. New actin filaments are formed by the cutting of existing filaments or de novo through the action of specialized nucleators. The most highly characterized nucleator is the Arp2/3 complex, which nucleates the branched actin networks in the lamellae of migrating cells. Recently, Bni1p, which is a member of the formin family of proteins, has been shown to nucleate actin filaments in vitro. Formins are implicated in the formation of actin cables in yeast, stress fibers in tissue culture cells and cytokinesis in many cell types. Formins contain two highly conserved formin-homology domains, FH1 and FH2. The Bni1p FH2 domain is sufficient to mediate nucleation. The Bni1p FH1 domain binds profilin, an actin-monomer-binding protein that delivers actin to the growing barbed end of filaments. The Bni1p FH1-profilin interaction enhances nucleation. Formins participate in a number of signaling pathways that control the assembly of specific actin structures and bind the barbed end of actin filaments, thereby providing a cytoskeletal basis for the establishment of cell polarity.

Key words: Formins, Bni1p, Cell polarity, Actin assembly, Signal transduction


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