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Role of insulin receptor substrate‐2 in interleukin‐9‐dependent proliferation
Author(s) -
Demoulin Jean-Baptiste,
Grasso Luigi,
Atkins John M.,
Stevens Monique,
Louahed Jamila,
Levitt Roy C.,
Nicolaides Nicholas C.,
Renauld Jean-Christophe
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02059-7
Subject(s) - phosphorylation , irs1 , irs2 , microbiology and biotechnology , insulin receptor substrate , signal transducing adaptor protein , phosphatidylinositol , insulin receptor , ectopic expression , protein kinase b , transfection , signal transduction , biology , chemistry , cell culture , endocrinology , insulin , insulin resistance , genetics
Interleukin‐9 (IL‐9) stimulation results in JAK, STAT and IRS1/2 phosphorylation. The role of IRS adaptor proteins in IL‐9 signaling is not clear. We show that IL‐9 induces IRS2 phosphorylation and association with phosphatidylinositol‐3 kinase (PI 3‐K) p85 subunit in TS1 cells and BaF/9R cells, which proliferate upon IL‐9 stimulation. We observed a PI 3‐K‐dependent phosphorylation of protein kinase B (PKB) in TS1 cells, but not in BaF/9R, nor in other IL‐9‐dependent cell lines. Finally, 32D cells that were transfected with the IL‐9 receptor but lack IRS expression survived in the presence of IL‐9. Ectopic IRS1 expression allowed for IL‐9‐induced proliferation, in the absence of significant PKB phosphorylation.