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Publication : Activation of the Drosophila NF-kappaB factor Relish by rapid endoproteolytic cleavage.

First Author  Stöven S Year  2000
Journal  EMBO Rep. Volume  1
Pages  347-52 PubMed ID  11269501
Abstract Text  The Rel/NF-kappaB transcription factor Relish plays a key role in the humoral immune response in Drosophila. We now find that activation of this innate immune response is preceded by rapid proteolytic cleavage of Relish into two parts. An N-terminal fragment, containing the DNA-binding Rel homology domain, translocates to the nucleus where it binds to the promoter of the Cecropin A1 gene and probably to the promoters of other antimicrobial peptide genes. The C-terminal IkappaB-like fragment remains in the cytoplasm. This endoproteolytic cleavage does not involve the proteasome, requires the DREDD caspase, and is different from previously described mechanisms for Rel factor activation. Doi  10.1093/embo-reports/kvd072
Issue  4 Month  Oct

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