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Multiple tyrosine residues in the intracellular domain of the common β subunit of the interleukin 5 receptor are involved in activation of STAT5
Author(s) -
van Dijk Thamar B,
Caldenhoven Eric,
Raaijmakers Jan A.M,
Lammers Jan-Willem J,
Koenderman Leo,
de Groot Rolf P
Publication year - 1997
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(97)00768-0
Subject(s) - tyrosine , intracellular , protein subunit , interleukin 12 receptor, beta 1 subunit , chemistry , interleukin 10 receptor, alpha subunit , stat5 , tyrosine kinase , receptor , interleukin 5 receptor alpha subunit , microbiology and biotechnology , biochemistry , biology , g alpha subunit , gene
In contrast to the general model of cytokine‐induced JAK/STAT signaling, tyrosine phosphorylation of the IL‐5R β chain seems to be dispensable for STAT activation in cells overexpressing exogenous STAT proteins. In this study we expressed IL‐5 receptor mutants in 293 cells and studied IL‐5‐induced endogenous STAT‐dependent transcription. Our results indicate that: (a) tyrosine phosphorylation of the IL‐5R β chain is required for endogenous STAT5 activation, (b) multiple tyrosine residues are phosphorylated upon IL‐5 stimulation, including Tyr 577 , Tyr 612 , Tyr 695 , and Tyr 750 , and (c) Tyr 612 , Tyr 695 , and Tyr 750 are all capable of inducing activation of STAT5, demonstrating a high level of functional redundancy within the IL‐5R β chain.