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

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 Lett

journal_title

FEBS letters

authors

Erhardt I,Lischke A,Sebald W,Friedrich K

doi

10.1016/s0014-5793(98)01341-6

subject

Has Abstract

pub_date

1998-11-13 00:00:00

pages

71-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)01341-6

journal_volume

439

pub_type

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