FEBS Letters | |
Multiple tyrosine residues in the intracellular domain of the common β subunit of the interleukin 5 receptor are involved in activation of STAT5 | |
Koenderman, Leo1  van Dijk, Thamar B1  de Groot, Rolf P1  Caldenhoven, Eric1  Lammers, Jan-Willem J1  Raaijmakers, Jan A.M1  | |
[1] Department of Pulmonary Diseases, University Hospital Utrecht, Heidelberglaan 100, 3584 CX Utrecht, Netherlands | |
关键词: IL-5; IL-3; GM-CSF receptor; Signaling; Stat protein; JAK; Janus kinase; STAT; signal transducer and activator of transcription; IL; interleukin; IL-5R; receptor for IL-5; GM-CSF; granulocyte macrophage colony-stimulating factor; IFN; interferon; SH domain; Src homology domain; ICAM-1; intercellular adhesion molecule-1; | |
DOI : 10.1016/S0014-5793(97)00768-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 Tyr577, Tyr612, Tyr695, and Tyr750, and (c) Tyr612, Tyr695, and Tyr750 are all capable of inducing activation of STAT5, demonstrating a high level of functional redundancy within the IL-5R β chain.
【 授权许可】
Unknown
【 预 览 】
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