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Caspase-mediated pr...
Caspase-mediated processing of the Drosophila NF-κB factor Relish
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Stöven, Svenja (författare)
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Silverman, Neil (författare)
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- Junell, Anna (författare)
- Stockholms universitet,Institutionen för molekylärbiologi och funktionsgenomik
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- Hedengren-Olcott, Marika (författare)
- Stockholms universitet,Wenner-Grens institut
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Erturk, Deniz (författare)
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- Engström, Ylva (författare)
- Stockholms universitet,Institutionen för molekylärbiologi och funktionsgenomik
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Maniatis, Tom (författare)
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Hultmark, Dan (författare)
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(creator_code:org_t)
- 2003-05-05
- 2003
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 100:10, s. 5991-5996
- Relaterad länk:
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https://europepmc.or...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The NF-κB-like transcription factor Relish plays a central role in the innate immune response of Drosophila. Unlike other NF-κB proteins, Relish is activated by endoproteolytic cleavage to generate a DNA-binding Rel homology domain and a stable IκB-like fragment. This signal-induced endoproteolysis requires the activity of several gene products, including the IκB 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 IκB-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 IκB kinase β. Finally, an N-terminal serine-rich region in Relish and the PEST domain were found to negatively regulate Relish activation.
Nyckelord
- NATURAL SCIENCES
- NATURVETENSKAP
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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