Abstract:
: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 alpha and gamma 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Erhardt I,Lischke A,Sebald W,Friedrich Kdoi
10.1016/s0014-5793(98)01341-6subject
Has Abstractpub_date
1998-11-13 00:00:00pages
71-4issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01341-6journal_volume
439pub_type
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