Forskning ved Københavns Universitet - Københavns Universitet

Forside

Surfing the insulin signaling web

Publikation: Bidrag til tidsskriftReviewForskningfagfællebedømt

  • E. Van Obberghen
  • V. Baron
  • L. Delahaye
  • Emanuelli, Brice
  • N. Filippa
  • S. Giorgetti-Peraldi
  • P. Lebrun
  • I. Mothe-Satney
  • P. Peraldi
  • S. Rocchi
  • D. Sawka-Verhelle
  • S. Tartare-Deckert
  • J. Giudicelli

The diverse biological actions of insulin and insulin-like growth factor I (IGF-I) are initiated by binding of the polypeptides to their respective cell surface tyrosine kinase receptors. These activated receptors phosphorylate a series of endogenous substrates on tyrosine, amongst which the insulin receptor substrate (IRS) proteins are the best characterized. Their phosphotyrosine-containing motifs become binding sites for Src homology 2 (SH2) domains on proteins such as SH2 domain-containing protein-tyrosine-phosphatase (SHP)-2/Syp, growth factor receptor bound-2 protien, (Grb-2), and phosphatidyl inositol 3 kinase (PI3 kinase), which participate in activation of specific signaling cascades. However, the IRS molecules are not only platforms for signaling molecules, they also orchestrate the generation of signal specificity, integration of signals induced by several extracellular stimuli, and signal termination and modulation. An extensive review is beyond the scope of the present article, which will be centered on our own contribution and reflect our biases.

OriginalsprogEngelsk
TidsskriftEuropean Journal of Clinical Investigation
Vol/bind31
Udgave nummer11
Sider (fra-til)966-977
Antal sider12
ISSN0014-2972
DOI
StatusUdgivet - 1 dec. 2001
Eksternt udgivetJa

ID: 200864724