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首页> 外文期刊>Molecular and Cellular Biology >A novel STAT-like factor mediates lipopolysaccharide, interleukin 1 (IL-1), and IL-6 signaling and recognizes a gamma interferon activation site-like element in the IL1B gene.
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A novel STAT-like factor mediates lipopolysaccharide, interleukin 1 (IL-1), and IL-6 signaling and recognizes a gamma interferon activation site-like element in the IL1B gene.

机译：一种新型的STAT样因子介导脂多糖，白介素1（IL-1）和IL-6信号传导，并识别IL1B基因中的γ干扰素激活位点样元件。

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Binding of many cytokines to their cognate receptors immediately activates Jak tyrosine kinases and their substrates, STAT (signal transducers and activators of transcription) DNA-binding proteins. The DNA binding targets of STATs are sequence elements related to the archetypal gamma interferon activation site, GAS. However, association of interleukin 1 (IL-1) with Jak-STAT signaling has remained unresolved. We now report an element termed LILRE (lipopolysaccharide [LPS] and IL-1-responsive element) in the human prointerleukin 1beta gene (IL1B) which can be immediately induced by either lipopolysaccharide (LPS) or IL-1 protein to bind a tyrosine-phosphorylated protein. This LPS- and IL-1-induced factor (LIL factor) is recognized by an antibody raised against the N terminus of Stat1, but not by those specific for either the C terminus of Stat1 or any other GAS-binding STAT. Phosphotyrosine (P-Tyr) specifically inhibits formation of the LIL factor-DNA complex, suggesting the importance of P-Tyr for the DNA-binding activity, as has been found for all STAT dimers. Analysis of DNA-binding specificity demonstrates that the LIL factor possesses a novel GAS-like binding activity that contrasts with those of other STATs in a requirement for a G residue at position 8 (TTCCTGAGA). Further investigation has revealed that IL-6, but neither IL-4 nor gamma interferon, activates the LIL factor. Thus, the existence of such a STAT-like factor (LIL-Stat) relates the LPS and IL-1 signaling pathway to other cytokine receptor signaling pathways via the activation of STATs. Moreover, the unique DNA-binding specificity and antigenicity of this factor suggest that LPS, IL-1, and IL-6 may use a common signaling pathway.
机译：许多细胞因子与其同源受体的结合会立即激活Jak酪氨酸激酶及其底物STAT（信号转导和转录激活剂）DNA结合蛋白。 STAT的DNA结合靶标是与原型伽马干扰素激活位点GAS相关的序列元件。然而，白细胞介素1（IL-1）与Jak-STAT信号传导的关联仍未解决。现在，我们报道了人类白细胞介素1beta基因（IL1B）中的一种称为LILRE（脂多糖[ILS]和IL-1应答元件）的元件，它可以立即由脂多糖（LPS）或IL-1蛋白诱导结合酪氨酸-磷酸化的蛋白质。该LPS和IL-1诱导因子（LIL因子）被针对Stat1 N端的抗体所识别，但未被针对Stat1 C端或任何其他GAS结合STAT的抗体所识别。磷酸酪氨酸（P-Tyr）特异性抑制LIL因子-DNA复合物的形成，表明P-Tyr对DNA结合活性的重要性，正如所有STAT二聚体所发现的那样。 DNA结合特异性的分析表明，LIL因子具有新颖的GAS样结合活性，与其他STATs的结合活性相反，它需要8位G残基（TTCCTGAGA）。进一步的研究表明，IL-6激活LIL因子，但IL-4和γ干扰素均不激活。因此，这种STAT样因子（LIL-Stat）的存在通过激活STATs将LPS和IL-1信号传导途径与其他细胞因子受体信号传导途径联系起来。此外，该因子独特的DNA结合特异性和抗原性表明LPS，IL-1和IL-6可能使用共同的信号通路。

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