Insulin promotes Rip11 accumulation at the plasma membrane by inhibiting a dynamin- and PI3-kinase-dependent, but Akt-independent, internalisation event.
Insulin promotes Rip11 accumulation at the plasma membrane by inhibiting a dynamin- and PI3-kinase-dependent, but Akt-independent, internalisation event.
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DOI：
10.1016/j.cellsig.2015.10.014
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发表时间：
2016-01
影响因子：
4.8
通讯作者：
Tavaré JM
中科院分区：
文献类型：
--
作者：
Boal F;Hodgson LR;Reed SE;Yarwood SE;Just VJ;Stephens DJ;McCaffrey MW;Tavaré JM
Rip 11是Rab 11效应蛋白，已被证明在控制几种细胞内货物的运输中是重要的，包括脂肪酸转运蛋白FAT/CD 36、V-ATP酶和葡萄糖转运蛋白GLUT 4。我们以前已经证明，Rip 11易位到质膜响应胰岛素，在这里，我们更详细地研究这种调节现象的基础。我们表明，Rip 11迅速之间的细胞内部和表面，胰岛素的能力，以增加Rip 11的外观在细胞表面涉及抑制Rip 11从质膜内化。相反，激素对Rip 11向质膜转运的速率没有影响。胰岛素抑制Rip 11内化的能力需要发动蛋白和I类PI 3激酶，但不依赖于蛋白激酶Akt的激活;其特征与胰岛素抑制GLUT 4内吞作用的机制非常相似。
Rip11 is a Rab11 effector protein that has been shown to be important in controlling the trafficking of several intracellular cargoes, including the fatty acid transporter FAT/CD36, V-ATPase and the glucose transporter GLUT4. We have previously demonstrated that Rip11 translocates to the plasma membrane in response to insulin and here we examine the basis of this regulated phenomenon in more detail. We show that Rip11 rapidly recycles between the cell interior and surface, and that the ability of insulin to increase the appearance of Rip11 at the cell surface involves an inhibition of Rip11 internalisation from the plasma membrane. By contrast the hormone has no effect on the rate of Rip11 translocation towards the plasma membrane. The ability of insulin to inhibit Rip11 internalisation requires dynamin and class I PI3-kinases, but is independent of the activation of the protein kinase Akt; characteristics which are very similar to the mechanism by which insulin inhibits GLUT4 endocytosis.