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  • Stöven, SvenjaUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten),Klinisk bakteriologi,Dan Hultmark (author)

Caspase-mediated processing of the Drosophila NF-kappaB factor Relish.

  • Article/chapterEnglish2003

Publisher, publication year, extent ...

  • 2003
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:umu-17059
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-17059URI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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.

Subject headings and genre

  • 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

Added entries (persons, corporate bodies, meetings, titles ...)

  • Silverman, Neal (author)
  • Junell, Anna (author)
  • Hedengren-Olcott, MarikaUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten),Dan Hultmark (author)
  • Erturk, Deniz (author)
  • Engstrom, Ylva (author)
  • Maniatis, Tom (author)
  • Hultmark, DanUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten),D(Swepub:umu)dahu0001 (author)
  • Umeå universitetUmeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten) (creator_code:org_t)

Related titles

  • In:Proc Natl Acad Sci U S A100:10, s. 5991-60027-8424

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