Naeger L K, McKinney J, Salvekar A, Hoey T
Tularik, Inc., South San Francisco, California 94080, USA.
J Biol Chem. 1999 Jan 22;274(4):1875-8. doi: 10.1074/jbc.274.4.1875.
The specificity of the various STAT SH2 domains for different tyrosine-containing peptides enables cytokines to activate different signaling pathways and 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 beta2 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 beta1 and beta2 subunits is sufficient for STAT4 activation but not for STAT1 or STAT3 activation.
各种STAT SH2结构域对不同含酪氨酸肽段的特异性，使得细胞因子能够激活不同的信号通路并诱导不同的基因表达模式。我们发现，STAT4具有独特的肽段特异性，能与肽序列pYLPSNID（其中pY代表磷酸酪氨酸）结合。该基序存在于白细胞介素-12受体β2亚基的酪氨酸残基800处，是STAT4的DNA结合和转录活性所必需的。我们的数据表明，转染白细胞介素-12受体β1和β2亚基足以激活STAT4，但不足以激活STAT1或STAT3。
