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Title: Latrunculin alters the actin-monomer subunit interface to prevent polymerization
Authors: Morton, Walter M
Ayscough, Kathryn R
McLaughlin, Paul J
Issue Date: Jun-2000
Citation: Latrunculin alters the actin-monomer subunit interface to prevent polymerization Morton WM, Ayscough KR, McLaughlin PJ NATURE CELL BIOLOGY 2 (6): 376-378 JUN 2000
Publisher: Nature Publishing Group
Abstract: Latrunculin-A is a drug that is capable of rapidly, reversibly and specifically disrupting the actin cytoskeleton. The efficacy of its action has made it a compound of choice in many cell-biology laboratories, supplanting the classic actin-depolymerizing drug cytochalasin-D. One reason for this is that the mode of action of latrunculin seems to be less complex than that of cytochalasin. Whereas the latter affects the kinetics of actin-filament polymerization at both the barbed and pointed ends, latrunculin-A seems to associate only with actin monomers, thereby preventing them from repolymerizing into filaments. The association of latrunculin with monomeric, rather than filamentous, actin gave us the opportunity to further our understanding of this interaction by detailed structural analysis of actin monomers using crystallographic techniques. Here we show the first high-resolution structure of an actin-disrupting drug in association with actin and discuss how its interactions with actin, and the conformational changes that its binding causes, may explain its mode of action within the cell.
Keywords: Latrunculin
URI: www.nature.com/ncb
doi:10.1038/35014075
http://hdl.handle.net/1842/757
Appears in Collections:Biological Sciences publications

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