Open AccessTyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases by interleukins 2 and 15.
Author(s) -
J. A. Johnston,
Chris M. Bacon,
D S Finbloom,
Robert C. Rees,
Daniel H. Kaplan,
Kengo Shibuya,
John R. Ortaldo,
Shan R. Gupta,
Y Q Chen,
Jayeeta Giri
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.19.8705
Subject(s) - tyrosine phosphorylation , stat5 , janus kinase , stat3 , phosphorylation , microbiology and biotechnology , jak stat signaling pathway , receptor tyrosine kinase , janus kinase 2 , stat , tyrosine kinase 2 , tyrosine kinase , signal transduction , biology , stat protein , sh2 domain , cancer research , receptor , biochemistry , platelet derived growth factor receptor , growth factor
The cytokines interleukin 2 (IL-2) and IL-15 have similar biological effects on T cells and bind common hematopoietin receptor subunits. Pathways that involve Janus kinases (JAKs) and signal transducers and activators of transcription (STATs) have been shown to be important for hematopoietin receptor signaling. In this study we identify the STAT proteins activated by IL-2 and IL-15 in human T cells. IL-2 and IL-15 rapidly induced the tyrosine phosphorylation of STAT3 and STAT5, and DNA-binding complexes containing STAT3 and STAT5 were rapidly activated by these cytokines in T cells. IL-4 induced tyrosine phosphorylation and activation of STAT3 but not STAT5. JAK1 and JAK3 were tyrosine-phosphorylated in response to IL-2 and IL-15. Hence, the JAK and STAT molecules that are activated in response to IL-2 and IL-15 are similar but differ from those induced by IL-4. These observations identify the STAT proteins activated by IL-2 and IL-15 and therefore define signaling pathways by which these T-cell growth factors may regulate gene transcription.