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Activation of the Drosophila NF‐κB factor Relish by rapid endoproteolytic cleavage
Author(s) -
Stöven Svenja,
Ando Istvan,
Kadalayil Latha,
Engström Ylva,
Hultmark Dan
Publication year - 2000
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kvd072
Subject(s) - transcription factor , biology , microbiology and biotechnology , promoter , innate immune system , gene , cecropin , schneider 2 cells , cleavage (geology) , proteasome , cytoplasm , transcription (linguistics) , nucleus , proteolysis , ubiquitin , genetics , immune system , gene expression , antimicrobial peptides , biochemistry , bacteria , rna interference , paleontology , fracture (geology) , rna , linguistics , philosophy , enzyme
The Rel/NF‐κB 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 IκB‐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.