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首页> 外文期刊>Molecular biology of the cell >Role of insulin-dependent cortical fodrin/spectrin remodeling in glucose transporter 4 translocation in rat adipocytes
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Role of insulin-dependent cortical fodrin/spectrin remodeling in glucose transporter 4 translocation in rat adipocytes

机译:胰岛素依赖性皮质铁蛋白/血影蛋白重塑在大鼠脂肪细胞葡萄糖转运蛋白4易位中的作用

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摘要

Fodrin or nonerythroid spectrin is an abundant component of the cortical cytoskeletal network in rat adipocytes. Fodrin has a highly punctate distribution in resting cells, and insulin causes a dramatic remodeling of fodrin to a more diffuse pattern. Insulin-mediated remodeling of actin occurs to a lesser extent than does that of fodrin. We show that fodrin interacts with the t-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) syntaxin 4, and this interaction is increased by insulin stimulation and decreased by prior latrunculin A treatment. Latrunculin A disrupts all actin filaments, inhibits glucose transporter 4 (GLUT4) translocation, and causes fodrin to partially redistribute from the plasma membrane to the cytosol. In contrast, cytochalasin D disrupts only the short actin filament signal, and cytochalasin D neither inhibits GLUT4 translocation nor fodrin redistribution in adipocytes. Together, our data suggest that insulin induces remodeling of the fodrin-actin network, which is required for the fusion of GLUT4 storage vesicles with the plasma membrane by permitting their access to the t-SNARE syntaxin 4.
机译:Fodrin或非类红血球蛋白是大鼠脂肪细胞中皮质细胞骨架网络的丰富组成部分。 Fodrin在静息细胞中具有高度的点状分布,胰岛素会导致fodrin急剧地重塑为更弥漫的模式。胰岛素介导的肌动蛋白重塑的发生程度少于铁蛋白。我们显示,铁蛋白与t-可溶性N-乙基马来酰亚胺敏感性因子附着蛋白受体(SNARE)syntaxin 4相互作用,并且这种相互作用通过胰岛素刺激而增加,并且通过先前的latrunculin A治疗而减少。 Latrunculin A破坏所有肌动蛋白丝,抑制葡萄糖转运蛋白4(GLUT4)易位,并导致fodrin从质膜部分重新分布到细胞质中。相反,细胞松弛素D仅破坏肌动蛋白丝短信号,而细胞松弛素D既不抑制GLUT4的转运,也不抑制其在脂肪细胞中的重新分布。总之,我们的数据表明胰岛素诱导了fodrin-actin网络的重塑,这是GLUT4存储囊泡与质膜融合所必需的,它允许它们进入t-SNARE语法4。

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