umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Caspase-mediated processing of the Drosophila NF-kappaB factor Relish.
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)
Show others and affiliations
2003 (English)In: Proc Natl Acad Sci U S A, ISSN 0027-8424, Vol. 100, no 10, 5991-6 p.Article in journal (Refereed) Published
Abstract [en]

The NF-kappaB-like transcription factor Relish plays a central role in the innate immune response of Drosophila. Unlike other NF-kappaB proteins, Relish is activated by endoproteolytic cleavage to generate a DNA-binding Rel homology domain and a stable IkappaB-like fragment. This signal-induced endoproteolysis requires the activity of several gene products, including the IkappaB kinase complex and the caspase Dredd. Here we used mutational analysis and protein microsequencing to demonstrate that a caspase target site, located in the linker region between the Rel and the IkappaB-like domain, is the site of signal-dependent cleavage. We also show physical interaction between Relish and Dredd, suggesting that Dredd indeed is the Relish endoprotease. In addition to the caspase target site, the C-terminal 107 aa of Relish are required for endoproteolysis and signal-dependent phosphorylation by the Drosophila IkappaB kinase beta. Finally, an N-terminal serine-rich region in Relish and the PEST domain were found to negatively regulate Relish activation.

Place, publisher, year, edition, pages
2003. Vol. 100, no 10, 5991-6 p.
Keyword [en]
Animals, Base Sequence, Caspases/*metabolism, Cells; Cultured, Chloramphenicol O-Acetyltransferase/genetics, DNA Primers, Drosophila Proteins/*genetics/metabolism, Drosophila melanogaster/*immunology, Gene Deletion, Gene Expression Regulation, Genes; Reporter, Kinetics, Molecular Sequence Data, Phosphorylation, Polymerase Chain Reaction, Sequence Deletion, Transcription Factors/*genetics/metabolism, beta-Galactosidase/genetics
Identifiers
URN: urn:nbn:se:umu:diva-17059PubMedID: 12732719OAI: oai:DiVA.org:umu-17059DiVA: diva2:156732
Available from: 2007-10-28 Created: 2007-10-28Bibliographically approved

Open Access in DiVA

No full text

Other links

PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=12732719&dopt=Citation

Authority records BETA

Stöven, SvenjaHultmark, Dan

Search in DiVA

By author/editor
Stöven, SvenjaHultmark, Dan
By organisation
Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Medicine)Clinical Bacteriology

Search outside of DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric score

pubmed
urn-nbn
Total: 92 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf