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Vol. 14, No. 19, pp. 2461-2471, October 1, 2000
B kinase complex required for Relish cleavage and antibacterial immunity
1 Department of Molecular and Cellular Biology, Harvard
University, Cambridge, Massachusetts 02138, USA; 2 Umeå
Center for Molecular Pathogenesis, Umeå University, S-901 87 Umeå, Sweden
Here we report the identification of a Drosophila I
B
kinase complex containing DmIKK
and DmIKK
, homologs of the
human IKK and IKK 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,
can phosphorylate Relish in vitro. Thus, we propose that the
Drosophila IB 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 IB 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 IB kinase complex must be required for Rel protein
activation via the Toll signaling pathway.
[Key Words:
insect immunity; NF-B; IKK; Relish]
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