Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Proc Natl Acad Sci U S A
2005 Feb 08;1026:1921-6. doi: 10.1073/pnas.0409062102.
Show Gene links
Show Anatomy links
Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.
Larson L, Arnaudeau S, Gibson B, Li W, Krause R, Hao B, Bamburg JR, Lew DP, Demaurex N, Southwick F.
???displayArticle.abstract???
The role of intracellular Ca2+ in the regulation of actin filament assembly and disassembly has not been clearly defined. We show that reduction of intracellular free Ca2+ concentration ([Ca2+]i) to <40 nM in Listeria monocytogenes-infected, EGFP-actin-transfected Madin-Darby canine kidney cells results in a 3-fold lengthening of actin filament tails. This increase in tail length is the consequence of marked slowing of the actin filament disassembly rate, without a significant change in assembly rate. The Ca2+-sensitive actin-severing protein gelsolin concentrates in the Listeria rocket tails at normal resting [Ca2+]i and disassociates from the tails when [Ca2+]i is lowered. Reduction in [Ca2+]i also blocks the severing activity of gelsolin, but not actin-depolymerizing factor (ADF)/cofilin microinjected into Listeria-infected cells. In Xenopus extracts, Listeria tail lengths are also calcium-sensitive, markedly shortening on addition of calcium. Immunodepletion of gelsolin, but not Xenopus ADF/cofilin, eliminates calcium-sensitive actin-filament shortening. Listeria tail length is also calcium-insensitive in gelsolin-null mouse embryo fibroblasts. We conclude that gelsolin is the primary Ca2+-sensitive actin filament recycling protein in the cell and is capable of enhancing Listeria actin tail disassembly at normal resting [Ca2+]i (145 nM). These experiments illustrate the unique and complementary functions of gelsolin and ADF/cofilin in the recycling of actin filaments.
Abe,
Xenopus laevis actin-depolymerizing factor/cofilin: a phosphorylation-regulated protein essential for development.
1996, Pubmed,
Xenbase
Abe,
Xenopus laevis actin-depolymerizing factor/cofilin: a phosphorylation-regulated protein essential for development.
1996,
Pubmed
,
Xenbase Allen,
Binding of phosphate, aluminum fluoride, or beryllium fluoride to F-actin inhibits severing by gelsolin.
1996,
Pubmed Arber,
Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase.
1998,
Pubmed Ballestrem,
Actin dynamics in living mammalian cells.
1998,
Pubmed Bamburg,
Proteins of the ADF/cofilin family: essential regulators of actin dynamics.
1999,
Pubmed Bengtsson,
Actin dynamics in human neutrophils during adhesion and phagocytosis is controlled by changes in intracellular free calcium.
1993,
Pubmed Carlier,
Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility.
1997,
Pubmed Carson,
An actin-nucleating activity in polymorphonuclear leukocytes is modulated by chemotactic peptides.
1986,
Pubmed Condeelis,
Life at the leading edge: the formation of cell protrusions.
1993,
Pubmed Cossart,
Actin-based bacterial motility.
1995,
Pubmed Cossart,
Bacterial invasion: the paradigms of enteroinvasive pathogens.
2004,
Pubmed Cunningham,
Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin.
1991,
Pubmed Dabiri,
Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly.
1990,
Pubmed De Corte,
Gelsolin-induced epithelial cell invasion is dependent on Ras-Rac signaling.
2002,
Pubmed Demaurex,
Regulation of Ca2+ influx in myeloid cells. Role of plasma membrane potential, inositol phosphates, cytosolic free [Ca2+], and filling state of intracellular Ca2+ stores.
1992,
Pubmed Dramsi,
Listeriolysin O-mediated calcium influx potentiates entry of Listeria monocytogenes into the human Hep-2 epithelial cell line.
2003,
Pubmed Greenberg,
Ca(2+)-independent F-actin assembly and disassembly during Fc receptor-mediated phagocytosis in mouse macrophages.
1991,
Pubmed Hartwig,
Mechanisms of actin rearrangements mediating platelet activation.
1992,
Pubmed Howard,
The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils.
1985,
Pubmed Janmey,
Cytoskeletal regulation: rich in lipids.
2004,
Pubmed Janmey,
Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking.
1985,
Pubmed Kumar,
Identification of a functional switch for actin severing by cytoskeletal proteins.
2004,
Pubmed Kwiatkowski,
Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain.
,
Pubmed Kwiatkowski,
Functions of gelsolin: motility, signaling, apoptosis, cancer.
1999,
Pubmed Laine,
Gelsolin, a protein that caps the barbed ends and severs actin filaments, enhances the actin-based motility of Listeria monocytogenes in host cells.
1998,
Pubmed Laine,
Vinculin proteolysis unmasks an ActA homolog for actin-based Shigella motility.
1997,
Pubmed Lew,
Modulation of cytosolic-free calcium transients by changes in intracellular calcium-buffering capacity: correlation with exocytosis and O2-production in human neutrophils.
1984,
Pubmed McGrath,
Regulation of the actin cycle in vivo by actin filament severing.
2000,
Pubmed Meshulam,
Calcium modulation and chemotactic response: divergent stimulation of neutrophil chemotaxis and cytosolic calcium response by the chemotactic peptide receptor.
1986,
Pubmed Nyakern-Meazza,
Tropomyosin and gelsolin cooperate in controlling the microfilament system.
2002,
Pubmed Rosenblatt,
Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails.
1997,
Pubmed
,
Xenbase Sanger,
Host cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes.
1992,
Pubmed Sidhu,
Phosphoinositide 3-kinase is required for intracellular Listeria monocytogenes actin-based motility and filopod formation.
2005,
Pubmed Sklar,
Signal transduction and ligand-receptor dynamics in the neutrophil. Ca2+ modulation and restoration.
1985,
Pubmed Southwick,
Gain-of-function mutations conferring actin-severing activity to human macrophage cap G.
1995,
Pubmed Stossel,
On the crawling of animal cells.
1993,
Pubmed Theriot,
The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization.
1992,
Pubmed Wadsworth,
Listeria monocytogenes phospholipase C-dependent calcium signaling modulates bacterial entry into J774 macrophage-like cells.
1999,
Pubmed Wallace,
Chemotactic peptide-induced changes in neutrophil actin conformation.
1984,
Pubmed White,
Stimulation by chemotactic factor of actin association with the cytoskeleton in rabbit neutrophils. Effects of calcium and cytochalasin B.
1983,
Pubmed Witke,
Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin.
1995,
Pubmed Yang,
Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization.
1998,
Pubmed Yin,
Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein.
1979,
Pubmed Zeile,
Recognition of two classes of oligoproline sequences in profilin-mediated acceleration of actin-based Shigella motility.
1996,
Pubmed
