A Drosophila IκB kinase complex required for Relish cleavage and antibacterial immunity

A Drosophila IκB kinase complex required for Relish cleavage and antibacterial immunity
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DOI:
10.1101/gad.817800
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发表时间:
2000-10-01
影响因子:
10.5
通讯作者:
Maniatis, T
Maniatis, T
中科院分区:
生物学1区
文献类型:
--
作者:
Silverman, N;Zhou, R;Maniatis, T

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在这里,我们报告的鉴定果蝇I κ B激酶复合物含有DmIKK β和DmIKK γ,同源的人IKK β和IKK γ蛋白。我们表明,这种复合物是必需的信号依赖性切割的Relish,一个成员的Rel家族的转录激活蛋白,并激活抗菌免疫反应基因。此外,我们发现激活的DmIKK复合物以及重组DmIKK β可以在体外磷酸化Relish。因此,我们建议,果蝇I κ B激酶复合物的功能,至少部分,通过诱导蛋白水解裂解的Relish。然后,Relish的N末端易位到细胞核并激活抗菌免疫应答基因的转录。值得注意的是,这种果蝇I κ B激酶复合物不是通过Toll信号通路激活Rel蛋白Dif和Dorsal所必需的,而Toll信号通路对于早期发育期间的抗真菌免疫和背腹图案化是必不可少的。因此,通过Toll信号传导途径活化Rel蛋白必须需要一种尚未鉴定的I κ B激酶复合物。
Here we report the identification of a Drosophila I kappa B kinase complex containing DmIKK beta and DmIKK gamma, homologs of the human IKK beta and IKK gamma proteins. We show that this complex is required for the signal-dependent cleavage of Relish, a member of the Rel family of transcriptional activator proteins, and for the activation of antibacterial immune response genes. In addition, we find that the activated DmIKK complex, as well as recombinant DmIKK beta, can phosphorylate Relish in vitro. Thus, we propose that the Drosophila I kappa B kinase complex functions, at least in part, by inducing the proteolytic cleavage of Relish. The N terminus of Relish then translocates to the nucleus and activates the transcription of antibacterial immune response genes. Remarkably, this Drosophila I kappa B kinase complex is not required for the activation of the Rel proteins Dif and Dorsal through the Toll signaling pathway, which is essential for antifungal immunity and dorsoventral patterning during early development. Thus, a yet to be identified I kappa B kinase complex must be required for Rel protein activation via the Toll signaling pathway.