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J. Biol. Chem., Vol. 277, Issue 51, 49205-49211, December 20, 2002
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From the T1/ST2 is a member of the interleukin
(IL)-1 receptor superfamily, possessing three immunoglobulin
domains extracellularly and a Toll/IL1R (TIR) domain intracellularly.
The ligand for T1/ST2 is not known. T1/ST2 is expressed on Type 2 T
helper (Th2) cells, and its role appears to be in the regulation of Th2
cell function. Here, we have investigated T1/ST2 signal transduction,
using either transient overexpression of T1/ST2 or a cross-linking
monoclonal antibody to activate cells. We demonstrate that T1/ST2 does
not activate the transcription factor NF-
Characterization of Signaling Pathways Activated by the
Interleukin 1 (IL-1) Receptor Homologue T1/ST2
A ROLE FOR JUN N-TERMINAL KINASE IN IL-4 INDUCTION*
§,¶,
,, and
Cytokine Research Group and the
Immunomodulation Group, Department of Biochemistry, Trinity
College, Dublin 2, Ireland and the ** Department of Biology,
Inflammation Division, Millennium Pharmaceuticals Inc.,
Cambridge, Massachusetts 02139
B when overexpressed in murine thymoma EL4 cells, or in the mast cell line P815 treated with
the anti-T1/ST2 antibody. However, a chimera comprising the extracellular domain of the type 1 IL-1 receptor and the intracellular domain of T1/ST2 activates NF-B both by overexpression and in response to IL-1. This artificial activation requires the IL1RAcP recruited via the extracellular portion (IL1R1) of the chimera. T1/ST2
is, however, able to activate the transcription factor activator
protein-1 (AP-1), increase phosphorylation of c-Jun, and
activate the MAP kinases c-Jun N-terminal kinase (JNK), p42/p44 and
p38. Anti-T1/ST2 also induces the selective expression of IL-4 but not
IFN-
in naive T cells. Importantly, this effect is blocked by prior
treatment with the JNK inhibitor SP600125 confirming that JNK as a key
effector in T1/ST2 signaling. The lack of effect on NF-B when T1/ST2
is homodimerized identifies T1/ST2 as the first member of the
IL-1 receptor superfamily so far studied that is apparently
unable to activate NF-B, consistent with evidence indicating the
lack of a role for NF-B in Th2 cell function.
*
This work was supported by grants from the Health Research
Board, Ireland, and Enterprise Ireland.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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