Actin Disassembly by Cofilin, Coronin, and Aip1 Occurs in Bursts and Is Inhibited by Barbed-end Cappers

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Actin Disassembly by Cofilin, Coronin, and Aip1 Occurs in Bursts and Is Inhibited by Barbed-end Cappers

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Title: Actin Disassembly by Cofilin, Coronin, and Aip1 Occurs in Bursts and Is Inhibited by Barbed-end Cappers
Author: Kueh, Hao Yuan; Charras, Guillaume T.; Brieher, William M.; Mitchison, Timothy J.

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Citation: Kueh, Hao Yuan, Guillaume T. Charras, Timothy J. Mitchison, and William M. Brieher. 2008. Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers. The Journal of Cell Biology 182(2): 341-353.
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Abstract: Turnover of actin filaments in cells requires rapid actin disassembly in a cytoplasmic environment that thermodynamically favors assembly because of high concentrations of polymerizable monomers. We here image the disassembly of single actin filaments by cofilin, coronin, and actin-interacting protein 1, a purified protein system that reconstitutes rapid, monomer-insensitive disassembly (Brieher, W.M., H.Y. Kueh, B.A. Ballif, and T.J. Mitchison. 2006. J. Cell Biol. 175:315–324). In this three-component system, filaments disassemble in abrupt bursts that initiate preferentially, but not exclusively, from both filament ends. Bursting disassembly generates unstable reaction intermediates with lowered affinity for CapZ at barbed ends. CapZ and cytochalasin D (CytoD), a barbed-end capping drug, strongly inhibit bursting disassembly. CytoD also inhibits actin disassembly in mammalian cells, whereas latrunculin B, a monomer sequestering drug, does not. We propose that bursts of disassembly arise from cooperative separation of the two filament strands near an end. The differential effects of drugs in cells argue for physiological relevance of this new disassembly pathway and potentially explain discordant results previously found with these drugs.
Published Version: doi:10.1083/jcb.200801027
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2483518/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:8347348

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