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Binding of IL‐4 to the IL‐13Rα 1 /IL‐4Rα receptor complex leads to STAT3 phosphorylation but not to its nuclear translocation
Author(s) -
Wery-Zennaro Sandrine,
Letourneur Martine,
David Muriel,
Bertoglio Jacques,
Pierre Josiane
Publication year - 1999
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(99)01680-4
Subject(s) - phosphorylation , tyrosine phosphorylation , interleukin 13 receptor , janus kinase , microbiology and biotechnology , stat protein , stat3 , signal transduction , jak stat signaling pathway , janus kinase 2 , phosphorylation cascade , janus kinase 1 , biology , receptor tyrosine kinase , chemistry , receptor , protein phosphorylation , biochemistry , protein kinase a , growth factor , insulin like growth factor 1 receptor
Interleukin‐4 (IL‐4) is a pleiotropic cytokine, which acts on both hematopoietic and non‐hematopoietic cells, through different types of receptor complexes. In this study, we report that in human B cells, IL‐4 caused rapid phosphorylation of Janus kinase (JAK) 1 and JAK3 tyrosine kinases. In keratinocytes, the hematopoietic‐specific receptor common γ c chain is not expressed and the IL‐13 receptor α 1 (IL‐13Rα 1 ) participates in IL‐4 signal transduction. In keratinocytes, IL‐4 induced JAK1 and JAK2 phosphorylation but, unlike in immune cells, IL‐4 did not involve JAK3 activation for its signaling. In both cell types, IL‐4 induced phosphorylation and DNA binding activation of the signal transducer and activator of transcription (STAT) 6 protein. Furthermore, IL‐4 stimulation of keratinocytes also induced tyrosine phosphorylation of STAT3 which was found to bind to the phosphorylated IL‐13Rα 1 . STAT3 however did not significantly translocate to the nucleus, nor did it bind with high affinity to target DNA sequences.