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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.
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Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

机译：凝溶胶蛋白介导李斯特菌肌动蛋白尾巴的钙依赖性拆解。

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摘要

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.
机译：细胞内Ca2 +在肌动蛋白丝组装和拆卸调控中的作用尚未明确。我们表明，在单核细胞增生李斯特氏菌感染的，EGFP-肌动蛋白转染的Madin-Darby犬肾细胞中，细胞内游离Ca2 +浓度（[Ca2 +] i）降低至<40 nM，导致肌动蛋白丝尾巴延长3倍。尾巴长度的增加是肌动蛋白丝分解速度明显减慢的结果，而组装速度没有显着变化。 Ca2 +敏感的肌动蛋白切断蛋白凝溶胶蛋白集中在正常静止的[Ca2 +] i处的李斯特菌火箭尾部，而当[Ca2 +] i降低时则从尾部解离。 [Ca2 +] i的减少也阻断凝溶胶蛋白的切断活性，但不会微注射到被李斯特菌感染的细胞中的肌动蛋白解聚因子（ADF）/ cofilin。在非洲爪蟾提取物中，李斯特菌的尾巴长度也对钙敏感，添加钙时会明显缩短。凝溶胶蛋白，而不是非洲爪蟾ADF / cofilin的免疫不全消除了钙敏感的肌动蛋白丝缩短。李斯特菌尾巴长度在凝溶胶蛋白无效的小鼠胚胎成纤维细胞中也不钙敏感。我们得出的结论是，凝溶胶蛋白是细胞中主要的Ca2 +敏感肌动蛋白丝再生蛋白，能够在正常静止[Ca2 +] i（145 nM）时增强李斯特菌肌动蛋白尾巴拆卸。这些实验说明了凝溶胶蛋白和ADF / cofilin在肌动蛋白丝回收中的独特和互补功能。

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