Gelsolin mediates calcium-dependent disassembly of Listeria actin tails

Article Article scientifique Article Gelsolin mediates calcium-dependent disassembly of Listeria actin tails eng 2005 author Larson Laura author Arnaudeau Serge 508253 author Gibson Bruce author Li Wei author Miyazaki-Krause Ryoko 27393 author Hao Binghua author Bamburg J. R. author Lew Daniel Pablo 26516 author Demaurex Nicolas 0000-0002-9933-6772 24642 author Southwick Frédérick 1921-1926 10.1073/pnas.0409062102 15671163 0027-8424 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC548556/pdf/pnas-0409062102.pdf 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. Actin Depolymerizing Factors Actins/genetics/ metabolism Animals Calcium/ metabolism Cells, Cultured Chelating Agents/metabolism Egtazic Acid/ analogs & derivatives/metabolism Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Gelsolin/ metabolism Listeria monocytogenes/cytology/ metabolism Mice Mice, Knockout Microfilament Proteins/metabolism Protein-Tyrosine Kinases/genetics/metabolism Recombinant Fusion Proteins/genetics/metabolism Xenopus laevis Dewey 616 56 Département de médecine 221 false Proceedings of the National Academy of Sciences of the United States of America 102 6 ad5795fe-eac2-4a29-8af7-778fb81d46cd Article Restricted file1.pdf 456507 application/pdf restrictedAccess Faculté de médecine / Section de médecine clinique / Département de médecine

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Gelsolin mediates calcium-dependent disassembly of Listeria actin tails	Proceedings of the National Academy of Sciences of the United States of America			2005	571	0

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Miyazaki-Krause, Ryoko