期刊
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
卷 33, 期 5, 页码 690-696出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2008.12.002
关键词
Innate immune response; Rel homology domain; I kappa B-like; Phosphorylation; Caspase cleavage; Scaffolding; Compound Rel protein; Antimicrobial peptide gene
资金
- Swedish Cancer Foundation
- Swedish Research Council
The Rel/NF-kappa B transcription factor Relish is a major regulator of the antimicrobial response in Drosophila. Upon immune challenge, Relish is cleaved to generate two fragments, the DNA-binding transcription factor REL-68 and the I kappa B-like REL-49. Using transgenic fly strains we show here that overexpression of REL-68 separately from REL-49 is sufficient to activate strong constitutive transcription of the Diptericin gene, but little constitutive or inducible transcription of Attacin and Cecropin, two other Relish target genes. Their transcription may therefore require additional modifications of Relish. However, phosphorylation of the conserved serine residue S431 is not involved in such modifications. This is unlike p65 and Dorsal, which are modulated by phosphorylation at their homologous site. In contrast to other I kappa B proteins, overexpression of REL-49 had no inhibitory effect on Relish-dependent transcription. Instead, we propose that the C-terminal I kappa B-like domain executes a scaffolding and recruiting function for full activation of Relish. (c) 2008 Elsevier Ltd. All rights reserved.
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