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Caspase-mediated processing of the Drosophila NF-kappaB factor Relish.
Umeå universitet, Medicinsk fakultet, Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten). Umeå universitet, Medicinsk fakultet, Klinisk mikrobiologi, Klinisk bakteriologi. (Dan Hultmark)
Umeå universitet, Medicinsk fakultet, Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten). (Dan Hultmark)
Vise andre og tillknytning
2003 (engelsk)Inngår i: Proc Natl Acad Sci U S A, ISSN 0027-8424, Vol. 100, nr 10, s. 5991-6Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2003. Vol. 100, nr 10, s. 5991-6
Emneord [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
Identifikatorer
URN: urn:nbn:se:umu:diva-17059PubMedID: 12732719OAI: oai:DiVA.org:umu-17059DiVA, id: diva2:156732
Tilgjengelig fra: 2007-10-28 Laget: 2007-10-28 Sist oppdatert: 2018-06-09bibliografisk kontrollert

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Stöven, SvenjaHultmark, Dan

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