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Ertürk-Hasdemir, D., Broemer, M., Leulier, F., Lane, W.S., Paquette, N., Hwang, D., Kim, C.H., Stöven, S., Meier, P., Silverman, N. (2009). Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes.  Proc. Natl. Acad. Sci. U.S.A. 106(24): 9779--9784.
FlyBase ID
FBrf0208153
Publication Type
Research paper
Abstract

The Drosophila NF-kappaB transcription factor Relish is an essential regulator of antimicrobial peptide gene induction after gram-negative bacterial infection. Relish is a bipartite NF-kappaB precursor protein, with an N-terminal Rel homology domain and a C-terminal IkappaB-like domain, similar to mammalian p100 and p105. Unlike these mammalian homologs, Relish is endoproteolytically cleaved after infection, allowing the N-terminal NF-kappaB module to translocate to the nucleus. Signal-dependent activation of Relish, including cleavage, requires both the Drosophila IkappaB kinase (IKK) and death-related ced-3/Nedd2-like protein (DREDD), the Drosophila caspase-8 like protease. In this report, we show that the IKK complex controls Relish by direct phosphorylation on serines 528 and 529. Surprisingly, these phosphorylation sites are not required for Relish cleavage, nuclear translocation, or DNA binding. Instead they are critical for recruitment of RNA polymerase II and antimicrobial peptide gene induction, whereas IKK functions noncatalytically to support Dredd-mediated cleavage of Relish.

PubMed ID
PubMed Central ID
PMC2701001 (PMC) (EuropePMC)
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Proc. Natl. Acad. Sci. U.S.A.
    Title
    Proceedings of the National Academy of Sciences of the United States of America
    Publication Year
    1915-
    ISBN/ISSN
    0027-8424
    Data From Reference
    Gene Groups (1)
    Genes (18)
    Physical Interactions (2)
    Cell Lines (1)