Constitutive association of JAK1 and STAT5 in pro‐B cells is dissolved by interleukin‐4‐induced tyrosine phosphorylation of both proteins

FEBS Letters

Friedrich, Karlheinz²  Lischke, Antje¹  Sebald, Walter²  Erhardt, Ingrid² 

[1]Max-Planck-Institut für Biologie, Corrensstr. 38, D-72076 Tübingen, Germany

[2]Theodor-Boveri-Institut für Biowissenschaften (Biozentrum), Physiologische Chemie II, Am Hubland, D-97074 Würzburg, Germany

关键词: Signal transduction;    Cytokine receptor;    JAK/STAT pathway;    Protein-protein interaction;    γc;    common receptor γ-chain;    DMEM;    Dulbecco's modified essential medium;    EPO;    erythropoietin;    FCS;    fetal calf serum;    G418;    geniticin;    GM-CSF;    granulocyte-macrophage colony-stimulating factor;    hIL-4;    human interleukin-4;    hIL-4R;    human interleukin-4 receptor;    mIL-4;    murine interleukin-4;    mIL-3;    murine interleukin-3;    hIL4Rα;    human interleukin-4 receptor α-subunit;    IgG;    immunoglobulin G;    IL;    interleukin;    JAK;    Janus kinase;    RPMI;    Rosswell Park Memorial Institute;    PCR;    polymerase chain reaction;    pTyr;    phosphotyrosine;    PTB domain;    phosphotyrosine binding domain;    SH2 domain;    src homology domain type 2;    STAT;    signal transducer and activator of transcription;   

DOI  :  10.1016/S0014-5793(98)01341-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The bipartite human interleukin-4 (IL-4) receptor was functionally expressed in murine pro-B cells and activated by human IL-4 to evoke intracellular signaling. Mutual association of signal transducing proteins within the receptor complex was then studied in dependence of ligand stimulation. Besides ligand-induced receptor heterodimerization and contacts of the two IL-4 receptor subunits α and γ with Janus kinases JAK1 and JAK3 a prominent constitutive binding between JAK1 and signal transducer and activator of transcription STAT5 was detected. Since both these proteins become phosphorylated in response to IL-4 receptor stimulation, the influence of tyrosine phosphorylation on their mutual contact was analyzed. Association of JAK1 and STAT5 was found to occur exclusively between unphosphorylated proteins.

【 授权许可】

Unknown