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Activation of the Drosophila NF-kappaB factor Relish by rapid endoproteolytic cleavage.
Umeå University, Faculty of Medicine, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Medicine). Umeå University, Faculty of Medicine, Clinical Microbiology, Clinical Bacteriology. (Dan Hultmark)
Umeå University, Faculty of Medicine, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Medicine). (Dan Hultmark)
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2000 (English)In: EMBO Rep, ISSN 1469-221X, Vol. 1, no 4, 347-52 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2000. Vol. 1, no 4, 347-52 p.
Keyword [en]
Animals, Blotting; Western, Caspases/metabolism, Drosophila Proteins, Drosophila melanogaster/*metabolism, Gene Expression, Genes; Insect, Insect Proteins/metabolism, NF-kappa B/*metabolism, Precipitin Tests, Signal Transduction, Transcription Factors/*metabolism
Identifiers
URN: urn:nbn:se:umu:diva-17068PubMedID: 11269501OAI: oai:DiVA.org:umu-17068DiVA: diva2:156741
Available from: 2007-10-28 Created: 2007-10-28Bibliographically approved

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PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=11269501&dopt=Citation

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Stöven, SvenjaHultmark, Dan

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