| http://purl.uniprot.org/citations/7782332 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7782332 | http://www.w3.org/2000/01/rdf-schema#comment | "The identification of JAK2 as a growth hormone (GH) receptor-associated, GH-activated tyrosine kinase has established tyrosyl phosphorylation as a signaling mechanism for GH. In the present study, GH is shown to stimulate tyrosyl phosphorylation of insulin receptor substrate 1 (IRS-1), the principle substrate of the insulin receptor. Tyrosyl phosphorylation of IRS-1 is a critical step in insulin signaling and provides binding sites for proteins with the appropriate Src homology 2 domains, including the 85-kDa regulatory subunit of phosphatidylinositol (PI) 3'-kinase. In 3T3-F442A fibroblasts, GH-dependent tyrosyl phosphorylation of IRS-1 was detected by 1 min and at GH concentrations as low as 5 ng/ml (0.23 nM). Tyrosyl phosphorylation of IRS-1 was transient, with maximal stimulation detected at 30 min and diminished signal detected at 60 min. The ability of GH receptor (GHR) to transduce the signal for IRS-1 tyrosyl phosphorylation is mediated by the intracellular region of GHR between amino acids 295 and 380 by a mechanism not involving the two tyrosines in this region. This region of GHR is required for GH-dependent JAK2 association and activation (VanderKuur, J. A., Wang, X., Zhang, L., Campbell, G. S., Allevato, G., Billestrup, N., Norstedt, G., and Carter-Su, C. (1994) J. Biol. Chem. 269, 21709-21717). When other cytokines that activate JAK2 were tested for the ability to stimulate the tyrosyl phosphorylation of IRS-1, stimulation was detected with interferon-gamma and leukemia inhibitory factor. The correlation between JAK2 tyrosyl phosphorylation and IRS-1 tyrosyl phosphorylation in response to GH, interferon-gamma, and leukemia inhibitory factor and in cells expressing different GHR mutants, provides evidence that IRS-1 may interact with JAK2 or an auxiliary molecule that binds to JAK2. GH is also shown to stimulate binding of IRS-1 to the 85-kDa regulatory subunit of PI 3'-kinase. The ability of GH to stimulate tyrosyl phosphorylation of IRS-1 and its association with PI 3'-kinase provides a biochemical basis for responses shared by insulin and GH including the well characterized insulin-like metabolic effects of GH observed in a variety of cell types."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.270.24.14685"xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/author | "White M.F."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/author | "Myers M.G. Jr."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/author | "Billestrup N."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/author | "Carter-Su C."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/author | "Argetsinger L.S."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/author | "Hsu G.W."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/pages | "14685-14692"xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/title | "Growth hormone, interferon-gamma, and leukemia inhibitory factor promoted tyrosyl phosphorylation of insulin receptor substrate-1."xsd:string |
| http://purl.uniprot.org/citations/7782332 | http://purl.uniprot.org/core/volume | "270"xsd:string |
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