Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 4594K) PPT slides of all figures Supplemental Material Index Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Google Scholar Articles by Kueh, H. Y. Articles by Brieher, W. M. PubMed PubMed Citation Articles by Kueh, H. Y. Articles by Brieher, W. M. Social Bookmarking                      What's this?

¹ Department of Systems Biology, Harvard Medical School, Boston, MA 02115
² Graduate Program in Biophysics, Harvard University, Cambridge, MA 02138
³ London Centre for Nanotechnology and ⁴ Department of Cell and Developmental Biology, Faculty of Life Sciences, University College London, London, England, UK
⁵ Department of Cell and Developmental Biology, University of Illinois, Urbana, IL 61801

Correspondence to William M. Brieher: wbrieher{at}uiuc.edu

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.

Abbreviations used in this paper: Aip1, actin-interacting protein 1; CCD, charge-coupled device; CytoD, cytochalasin D; df, degrees of freedom; KabC, kabiramide C; LatB, latrunculin B; PAGFP, photoactivatable GFP; mRFP, monomeric red fluorescence protein.

© 2008 Kueh et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Kueh, H. Y., Brieher, W. M., Mitchison, T. J. (2008). Dynamic stabilization of actin filaments. Proc. Natl. Acad. Sci. USA 105: 16531-16536 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents