Insulin elicits a ROS-activated and an IP₃-dependent Ca²⁺ release, which both impinge on GLUT4 translocation.

@article{ContrerasFerrat2014InsulinEA,
  title={Insulin elicits a ROS-activated and an IP₃-dependent Ca²⁺ release, which both impinge on GLUT4 translocation.},
  author={Ariel E. Contreras-Ferrat and Paola Llanos and Rosales V{\'a}squez and Alejandra Espinosa and C{\'e}sar Osorio-Fuentealba and Manuel Arias-Calder{\'o}n and Sergio Lavandero and Amira Klip and Cecilia Hidalgo and Enrique Jaimovich},
  journal={Journal of cell science},
  year={2014},
  volume={127 Pt 9},
  pages={
          1911-23
        }
}
Insulin signaling includes generation of low levels of H2O2; however, its origin and contribution to insulin-stimulated glucose transport are unknown. We tested the impact of H2O2 on insulin-dependent glucose transport and GLUT4 translocation in skeletal muscle cells. H2O2 increased the translocation of GLUT4 with an exofacial Myc-epitope tag between the first and second transmembrane domains (GLUT4myc), an effect additive to that of insulin. The anti-oxidants N-acetyl L-cysteine and Trolox… CONTINUE READING

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Signal transduction meets vesicle traffic: the software and hardware of GLUT4 translocation.

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