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Activation of the Drosophila NF‐κB factor Relish by rapid endoproteolytic cleavage

Open access
Stöven, Svenja, Ando, Istvan, Kadalayil, Latha, Engström, Ylva, Hultmark, Dan·2000·EMBO reports

Abstract

The Rel/NF‐κB 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 IκB‐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.

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Metadata

Authors
Stöven, S., Ando, I., Kadalayil, L., Engström, Y., & Hultmark, D.
Venue
EMBO reports
Published
2000-10
Volume
1
Issue
4
Pages
347-352
ISSN
  • 1469-221X (ISSN-L)
  • 1469-3178
OpenAlex
W2048869977
Cited by
338
References
0
FWCI
6.98
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Activation of the Drosophila NF‐κB factor Relish by rapid endoproteolytic cleavage. https://app.cochat.ai/papers/10.1093/embo-reports/kvd072
The paper
Stöven, S., Ando, I., Kadalayil, L., Engström, Y., & Hultmark, D. (2000). Activation of the Drosophila NF‐κB factor Relish by rapid endoproteolytic cleavage. EMBO reports. https://doi.org/10.1093/embo-reports/kvd072

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.