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Vol. 15, No. 15, pp. 1900-1912, August 1, 2001
B-dependent innate immune responses
1 Centre de Génétique Moléculaire, CNRS,
91198 Gif-sur-Yvette, France; 2 National Institute for Basic
Biology, Okasaki 444-8585, Japan
In mammals, TAK1, a MAPKKK kinase, is implicated in multiple
signaling processes, including the regulation of NF-
B activity via
the IL1-R/TLR pathways. TAK1 function has largely been studied in
cultured cells, and its in vivo function is not fully understood. We
have isolated null mutations in the Drosophila dTAK1 gene that encodes dTAK1, a homolog of TAK1. dTAK1 mutant flies are viable and fertile, but they do not produce antibacterial peptides and are
highly susceptible to Gram-negative bacterial infection. This phenotype
is similar to the phenotypes generated by mutations in components of
the Drosophila Imd pathway. Our genetic studies also indicate
that dTAK1 functions downstream of the Imd protein and upstream of the
IKK complex in the Imd pathway that controls the Rel/NF-B like
transactivator Relish. In addition, our epistatic analysis places the
caspase, Dredd, downstream of the IKK complex, which supports the idea
that Relish is processed and activated by a caspase activity. Our
genetic demonstration of dTAK1's role in the regulation of
Drosophila antimicrobial peptide gene expression suggests an
evolutionary conserved role for TAK1 in the activation of
Rel/NF-B-mediated host defense reactions.
[Key Words:
Innate immunity; antimicrobial peptide; rel/NF-B; Toll; TAK1; caspase]
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