1. Insulin promotes Rip11 accumulation at the plasma membrane by inhibiting a dynamin- and PI3-kinase-dependent, but Akt-independent, internalisation event.
- Author
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Boal F, Hodgson LR, Reed SE, Yarwood SE, Just VJ, Stephens DJ, McCaffrey MW, and Tavaré JM
- Subjects
- Adipocytes metabolism, Animals, Glucose Transporter Type 4 metabolism, Insulin metabolism, Mice, Phosphatidylinositol 3-Kinases metabolism, Phosphorylation, Protein Transport physiology, Proto-Oncogene Proteins c-akt metabolism, rab GTP-Binding Proteins, Carrier Proteins metabolism, Cell Membrane metabolism, Insulin pharmacology, Mitochondrial Proteins metabolism, Phosphatidylinositol 3-Kinases drug effects, Protein Transport drug effects
- Abstract
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., (Copyright © 2015. Published by Elsevier Inc.)
- Published
- 2016
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