Multiple tyrosine residues in the intracellular domain of the common β subunit of the interleukin 5 receptor are involved in activation of STAT5

FEBS Letters

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