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Gene Review

ird5  -  immune response deficient 5

Drosophila melanogaster

Synonyms: CG4201, Cactus kinase IKK, DIK, DLAK, DmIKK, ...
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Disease relevance of ird5

  • Consistent with this finding, Escherichia coli survive 100 times better in ird5 adults than in wild-type animals [1].

High impact information on ird5

  • However, DmIKK epsilon-mediated degradation of DIAP1 does not regulate apoptosis as might be predicted but instead regulates actin dynamics, cell morphology, and the differentiation of sensory organ precursor cells [2].
  • The ird5 phenotype and sequence suggest that the gene is specifically required for the activation of Relish, a Drosophila NF-kappaB family member [1].
  • Here we report the identification of a Drosophila IkappaB kinase complex containing DmIKKbeta and DmIKKgamma, homologs of the human IKKbeta and IKKgamma proteins [3].
  • We show here that crosstalk occurred between the drosophila Jnk and IKK pathways, which led to downregulation of each other's activity [4].
  • IkappaB kinase (IKK) and Jun N-terminal kinase (Jnk) signaling modules are important in the synthesis of immune effector molecules during innate immune responses against lipopolysaccharide and peptidoglycan [4].

Biological context of ird5

  • The DLAK(K50A) mutant also inhibits nuclear kappaB binding activity and kappaB-dependent diptericin reporter gene activity in a dose-dependent manner, but the kappaB-dependent diptericin reporter gene activity can be rescued by overexpression of wild type DLAK [5].
  • Two new papers (Kuranaga et al., 2006; Oshima et al., 2006) describe a previously uncharacterized Drosophila kinase (DmIKK epsilon) that regulates the abundance of DIAP1, a protein best known for its ability to inhibit apoptosis [2].
  • These findings place photoreceptor K+ channels as an additional target for Ca2+/calmodulin and suggest that IK is well suited to act in concert with other components of the signaling machinery to sharpen light response termination and fine tune photoreceptor sensitivity during light adaptation [6].
  • Likewise, inhibition of CaM kinases by KN-93 potently depressed IK and accelerated its C-type inactivation kinetics [6].
  • IKK epsilon regulates F actin assembly and interacts with Drosophila IAP1 in cellular morphogenesis [7].

Anatomical context of ird5

  • These data suggest that this IkappaB kinase has an NF-kappaB-independent role in mRNA localization and helps to link microtubule minus-ends to the oocyte cortex, a novel function of the IKK family [8].
  • Counteracting the light-activated depolarizing current are two voltage-gated K+ conductances, IA and IK, that are expressed in these sensory neurons [6].
  • Drosophila IKK epsilon was localized to the ruffling membrane of cultured cells and was required for F actin turnover at the cell margin [7].

Associations of ird5 with chemical compounds


Physical interactions of ird5

  • DLAK-bound Cactus can be degraded in a LPS signal-dependent fashion, whereas the DLAK(K50A) mutant-bound Cactus is completely resistant to degradation in the presence of LPS [5].
  • Activation of the DmIKK complex requires the MAP3K dTAK1, but the mechanism of dTAK1 activation is not understood [9].

Regulatory relationships of ird5

  • Overexpression of dominant-negative mutant DLAK (DLAK(K50A)) blocks LPS-induced Cactus degradation [5].

Other interactions of ird5

  • In addition, we find that the activated DmIKK complex, as well as recombinant DmIKKbeta, can phosphorylate Relish in vitro [3].
  • Here we demonstrate that the Drosophila homologs of Ubc13 and UEV1a are similarly required for the activation of dTAK1 and the DmIKK complex [9].
  • We show that imd functions upstream of the DmIKK signalosome and the caspase DREDD in the control of antibacterial peptide genes [10].


  1. The antibacterial arm of the drosophila innate immune response requires an IkappaB kinase. Lu, Y., Wu, L.P., Anderson, K.V. Genes Dev. (2001) [Pubmed]
  2. A kinase gets caspases into shape. Montell, D.J. Cell (2006) [Pubmed]
  3. A Drosophila IkappaB kinase complex required for Relish cleavage and antibacterial immunity. Silverman, N., Zhou, R., Stöven, S., Pandey, N., Hultmark, D., Maniatis, T. Genes Dev. (2000) [Pubmed]
  4. Downregulation of lipopolysaccharide response in Drosophila by negative crosstalk between the AP1 and NF-kappaB signaling modules. Kim, T., Yoon, J., Cho, H., Lee, W.B., Kim, J., Song, Y.H., Kim, S.N., Yoon, J.H., Kim-Ha, J., Kim, Y.J. Nat. Immunol. (2005) [Pubmed]
  5. Lipopolysaccharide-activated kinase, an essential component for the induction of the antimicrobial peptide genes in Drosophila melanogaster cells. Kim, Y.S., Han, S.J., Ryu, J.H., Choi, K.H., Hong, Y.S., Chung, Y.H., Perrot, S., Raibaud, A., Brey, P.T., Lee, W.J. J. Biol. Chem. (2000) [Pubmed]
  6. A Ca2+/calmodulin-dependent protein kinase modulates Drosophila photoreceptor K+ currents: a role in shaping the photoreceptor potential. Peretz, A., Abitbol, I., Sobko, A., Wu, C.F., Attali, B. J. Neurosci. (1998) [Pubmed]
  7. IKK epsilon regulates F actin assembly and interacts with Drosophila IAP1 in cellular morphogenesis. Oshima, K., Takeda, M., Kuranaga, E., Ueda, R., Aigaki, T., Miura, M., Hayashi, S. Curr. Biol. (2006) [Pubmed]
  8. Drosophila Ik2, a member of the I{kappa}B kinase family, is required for mRNA localization during oogenesis. Shapiro, R.S., Anderson, K.V. Development (2006) [Pubmed]
  9. The role of ubiquitination in Drosophila innate immunity. Zhou, R., Silverman, N., Hong, M., Liao, D.S., Chung, Y., Chen, Z.J., Maniatis, T. J. Biol. Chem. (2005) [Pubmed]
  10. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis. Georgel, P., Naitza, S., Kappler, C., Ferrandon, D., Zachary, D., Swimmer, C., Kopczynski, C., Duyk, G., Reichhart, J.M., Hoffmann, J.A. Dev. Cell (2001) [Pubmed]
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