PMID- 11737239 OWN - NLM STAT- MEDLINE DCOM- 20020412 LR - 20190826 IS - 0014-2972 (Print) IS - 0014-2972 (Linking) VI - 31 IP - 11 DP - 2001 Nov TI - Surfing the insulin signaling web. PG - 966-77 AB - 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 protein, (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. FAU - Van Obberghen, E AU - Van Obberghen E AD - Inserm U 145, IFR 50, Faculte de Medecine, Avenue de Valombrose, Nice Cedex, France. vanobbeg@unice.fr FAU - Baron, V AU - Baron V FAU - Delahaye, L AU - Delahaye L FAU - Emanuelli, B AU - Emanuelli B FAU - Filippa, N AU - Filippa N FAU - Giorgetti-Peraldi, S AU - Giorgetti-Peraldi S FAU - Lebrun, P AU - Lebrun P FAU - Mothe-Satney, I AU - Mothe-Satney I FAU - Peraldi, P AU - Peraldi P FAU - Rocchi, S AU - Rocchi S FAU - Sawka-Verhelle, D AU - Sawka-Verhelle D FAU - Tartare-Deckert, S AU - Tartare-Deckert S FAU - Giudicelli, J AU - Giudicelli J LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Review PL - England TA - Eur J Clin Invest JT - European journal of clinical investigation JID - 0245331 RN - 0 (Adaptor Proteins, Signal Transducing) RN - 0 (DNA-Binding Proteins) RN - 0 (GAB1 protein, human) RN - 0 (Insulin) RN - 0 (Integrins) RN - 0 (Milk Proteins) RN - 0 (Phosphoproteins) RN - 0 (Proteins) RN - 0 (Repressor Proteins) RN - 0 (SOCS3 protein, human) RN - 0 (STAT5 Transcription Factor) RN - 0 (Suppressor of Cytokine Signaling 3 Protein) RN - 0 (Suppressor of Cytokine Signaling Proteins) RN - 0 (Trans-Activators) RN - 0 (Transcription Factors) RN - 67763-96-6 (Insulin-Like Growth Factor I) RN - EC 2.7.10.1 (Receptor, IGF Type 1) SB - IM MH - Adaptor Proteins, Signal Transducing MH - Animals MH - DNA-Binding Proteins/metabolism MH - Humans MH - Insulin/*metabolism MH - Insulin-Like Growth Factor I/metabolism MH - Integrins/metabolism MH - *Milk Proteins MH - Models, Biological MH - Phosphoproteins/metabolism MH - Protein Structure, Tertiary MH - Proteins/metabolism MH - Receptor, IGF Type 1/*metabolism MH - *Repressor Proteins MH - STAT5 Transcription Factor MH - Signal Transduction/*physiology MH - Suppressor of Cytokine Signaling 3 Protein MH - Suppressor of Cytokine Signaling Proteins MH - Trans-Activators/metabolism MH - *Transcription Factors RF - 87 EDAT- 2001/12/12 10:00 MHDA- 2002/04/16 10:01 CRDT- 2001/12/12 10:00 PHST- 2001/12/12 10:00 [pubmed] PHST- 2002/04/16 10:01 [medline] PHST- 2001/12/12 10:00 [entrez] AID - 896 [pii] AID - 10.1046/j.1365-2362.2001.00896.x [doi] PST - ppublish SO - Eur J Clin Invest. 2001 Nov;31(11):966-77. doi: 10.1046/j.1365-2362.2001.00896.x.