Identification of a STAT4 binding site in the interleukin-12 receptor required for signaling

被引：62

作者：

Naeger, LK ^{[1
]}

McKinney, J ^{[1
]}

Salvekar, A ^{[1
]}

Hoey, T ^{[1
]}

机构：

[1] Tularik Inc, S San Francisco, CA 94080 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1999年 / 274卷 / 04期

关键词：

D O I：

10.1074/jbc.274.4.1875

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The specificity of the various STAT SH2 domains for different tyrosine-containing peptides enables cytokines to activate different signaling pathways rand to induce distinct patterns of gene expression. We show that STAT4 has a unique peptide specificity and binds to the peptide sequence pYLPSNID (where pY represents phosphotyrosine). This motif is found at tyrosine residue 800 in the beta 2 subunit of the interleukin-12 receptor and is required for DNA binding and transcriptional activity of STAT4, Our data demonstrate that transfection of interleukin-12 receptor beta 1 and beta 2 subunits is sufficient for STAT4 activation but not for STAT1 or STAT3 activation.

引用

页码：1875 / 1878

页数：4

共 35 条

[1] INTERLEUKIN-12 (IL-12) INDUCES TYROSINE PHOSPHORYLATION OF JAK2 AND TYK2 - DIFFERENTIAL USE OF JANUS FAMILY TYROSINE KINASES BY IL-2 AND IL-12 [J].