Details

Autor(en) / Beteiligte

• Antje Lischke
• Richard Moriggl
• Stephanie Brändlein
• Susanne Berchtold
• Winfried Kammer
• Walter Sebald
• Bernd Groner
• Xiuwen Liu
• Lothar Hennighausen
• Karlheinz Friedrich

Titel

The Interleukin-4 Receptor Activates STAT5 by a Mechanism That Relies upon Common γ-Chain

Ist Teil von

• The Journal of biological chemistry, 1998-11, Vol.273 (47), p.31222

Ort / Verlag

American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1998

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Interleukin (IL)-4 signaling proceeds via cytoplasmic activation of the Janus kinases JAK1 and JAK3 and the signal transducer and activator of transcription STAT6. We show that the IL-4 receptor, like other cytokine receptor systems utilizing the common receptor γ-chain (γc), is also connected to a signaling pathway that involves STAT5. Both STAT5a and STAT5b become tyrosine-phosphorylated and acquire specific DNA-binding properties in response to IL-4 receptor stimulation in the murine pro-B cell line Ba/F3. In preactivated human T cells, STAT5 became activated in an IL-4-dependent fashion as assayed by IL-4-induced STAT5 translocation from the cytoplasm to the cell nucleus and by binding to cognate DNA. Moreover, stimulation of preactivated human T cells by IL-4 led to specific transcriptional up-regulation of STAT5 target genes. IL-4 receptor-mediated STAT5 activation is dependent on the presence of γc and JAK3 within the receptor complex. In COS-7 cells, the JAK/STAT pathway leading from the IL-4 receptor to STAT5-dependent regulation of a reporter gene relied largely on coexpression of JAK3. In Ba/F3 cells, studies on signal transduction evoked by directed specific receptor homo- or heterodimerization revealed that STAT5 activation can be triggered exclusively by IL-4R heterodimers containing γc.