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Insulin signaling and the regulation of glucose transport.

Authors
  • Chang, Louise1
  • Chiang, Shian-Huey
  • Saltiel, Alan R
  • 1 Life Sciences Institute, Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109-2216, USA.
Type
Published Article
Journal
Molecular medicine (Cambridge, Mass.)
Publication Date
2004
Volume
10
Issue
7-12
Pages
65–71
Identifiers
PMID: 16307172
Source
Medline
License
Unknown

Abstract

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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