Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes.

@article{ErtrkHasdemir2009TwoRF,
  title={Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes.},
  author={Deniz Ert{\"u}rk-Hasdemir and Meike Broemer and François Leulier and William S. Lane and Nicholas R Paquette and Daye Hwang and Chan-Hee Kim and Svenja St{\"o}ven and Pascal C. H. Meier and Neal Silverman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 24},
  pages={9779-84}
}
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… CONTINUE READING
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The N-terminal half of the Drosophila Rel/NF-kappaB factor Relish, REL-68, constitutively activates transcription of specific Relish target genes

  • ML Wiklund
  • Dev Comp Immunol
  • 2009

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