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Publication Detail
The natural product cucurbitacin E inhibits depolymerization of actin filaments.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Sörensen PM, Iacob RE, Fritzsche M, Engen JR, Brieher WM, Charras G, Eggert US
  • Publication date:
    21/09/2012
  • Pagination:
    1502, 1508
  • Journal:
    ACS Chem Biol
  • Volume:
    7
  • Issue:
    9
  • Status:
    Published
  • Country:
    United States
  • Language:
    eng
  • Keywords:
    Actin Cytoskeleton, Actins, Animals, Biological Products, Cucurbitaceae, Depsipeptides, HeLa Cells, Humans, Polymerization, Rabbits, Triterpenes
Abstract
Although small molecule actin modulators have been widely used as research tools, only one cell-permeable small molecule inhibitor of actin depolymerization (jasplakinolide) is commercially available. We report that the natural product cucurbitacin E inhibits actin depolymerization and show that its mechanism of action is different from jasplakinolide. In assays using pure fluorescently labeled actin, cucurbitacin E specifically affects depolymerization without affecting polymerization. It inhibits actin depolymerization at substoichiometric concentrations up to 1:6 cucurbitacin E:actin. Cucurbitacin E specifically binds to filamentous actin (F-actin) forming a covalent bond at residue Cys257, but not to monomeric actin (G-actin). On the basis of its compatibility with phalloidin staining, we show that cucurbitacin E occupies a different binding site on actin filaments. Using loss of fluorescence after localized photoactivation, we found that cucurbitacin E inhibits actin depolymerization in live cells. Cucurbitacin E is a widely available plant-derived natural product, making it a useful tool to study actin dynamics in cells and actin-based processes such as cytokinesis.
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