Molecular Medicine

, Volume 10, Issue 7–12, pp 65–71 | Cite as

Insulin Signaling and the Regulation of Glucose Transport

  • Louise Chang
  • Shian-Huey Chiang
  • Alan R Saltiel
In Overview


Gaps remain in our understanding of the precise molecular mechanisms by which insulin regulates glucose uptake in fat and muscle cells. Recent evidence suggests that insulin action involves multiple pathways, each compartmentalized in discrete domains. Upon activation, the receptor catalyzes the tyrosine phosphorylation of a number of substrates. One family of these, the insulin receptor substrate (IRS) proteins, initiates activation of the phosphatidylinositol 3-kinase pathway, resulting in stimulation of protein kinases such as Akt and atypical protein kinase C. The receptor also phosphorylates the adapter protein APS, resulting in the activation of the G protein TC10, which resides in lipid rafts. TC10 can influence a number of cellular processes, including changes in the actin cytoskeleton, recruitment of effectors such as the adapter protein CIP4, and assembly of the exocyst complex. These pathways converge to control the recycling of the facilitative glucose transporter Glut4.


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Copyright information

© Feinstein Institute for Medical Research 2004

Authors and Affiliations

  • Louise Chang
    • 1
  • Shian-Huey Chiang
    • 1
  • Alan R Saltiel
    • 1
  1. 1.Life Sciences Institute, Departments of Internal Medicine and PhysiologyUniversity of MichiganAnn ArborUSA

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