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Inhibitor of apoptosis 2 and TAK1‐binding protein are components of the Drosophila Imd pathway
Author(s) -
Kleino Anni,
Valanne Susanna,
Ulvila Johanna,
Kallio Jenni,
Myllymäki Henna,
Enwald Heidi,
Stöven Svenja,
Poidevin Mickael,
Ueda Ryu,
Hultmark Dan,
Lemaitre Bruno,
Rämet Mika
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600807
Subject(s) - biology , schneider 2 cells , rna interference , microbiology and biotechnology , signal transduction , transcription factor , inhibitor of apoptosis , drosophila melanogaster , kinase , tor signaling , apoptosis , gene , programmed cell death , genetics , rna
The Imd signaling cascade, similar to the mammalian TNF‐receptor pathway, controls antimicrobial peptide expression in Drosophila . We performed a large‐scale RNAi screen to identify novel components of the Imd pathway in Drosophila S2 cells. In all, 6713 dsRNAs from an S2 cell‐derived cDNA library were analyzed for their effect on Attacin promoter activity in response to Escherichia coli . We identified seven gene products required for the Attacin response in vitro , including two novel Imd pathway components: inhibitor of apoptosis 2 (Iap2) and transforming growth factor‐activated kinase 1 (TAK1)‐binding protein (TAB). Iap2 is required for antimicrobial peptide response also by the fat body in vivo . Both these factors function downstream of Imd. Neither TAB nor Iap2 is required for Relish cleavage, but may be involved in Relish nuclear localization in vitro , suggesting a novel mode of regulation of the Imd pathway. Our results show that an RNAi‐based approach is suitable to identify genes in conserved signaling cascades.