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Gene Review

Iap2  -  Inhibitor of apoptosis 2

Drosophila melanogaster

Synonyms: Apoptosis 2 inhibitor, CG8293, D-IAP2, D-iap2, DIAP, ...
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Disease relevance of Iap2


High impact information on Iap2

  • Destabilizing influences in apoptosis: sowing the seeds of IAP destruction [5].
  • The inhibitor-of-apoptosis (IAP) proteins suppress cell death by inhibiting the activity of caspases; this inhibition is performed by the zinc-binding BIR domains of the IAP proteins [6].
  • This response is preceded by an ecdysone-triggered switch in gene expression in which the diap2 death inhibitor is repressed and the reaper (rpr) and head involution defective (hid) death activators are induced [7].
  • 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 [8].
  • Iap2 is required for antimicrobial peptide response also by the fat body in vivo [8].

Chemical compound and disease context of Iap2


Biological context of Iap2

  • 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) [8].
  • Increasing the genetic dose of diap2 results in an increased immune response, whereas expression of Rpr or Hid results in down-regulation of DIAP2 protein levels [1].
  • We also show that in both the midline and eye, grim-induced cell death is not blocked by the Drosophila anti-apoptosis protein Diap2, which does block both reaper- and hid-induced cell death. grim can also function synergistically with reaper or hid to induce higher levels of midline cell death than observed for any of the genes individually [9].
  • The phenotype of these mice suggests that it is the protease function of this protein and not its IAP binding motif that is critical [10].
  • Whereas loss of DIAP 1, the other member of the IAP protein family in Drosophila, leads to apoptosis, we show that IAP 2 is dispensable for cell viability in haemocyte-like cells [11].

Anatomical context of Iap2

  • The anti-apoptotic activities of two baculovirus IAPs, OpIAP and CpIAP, were directly compared with that of two Drosophila IAPs, DIAP1 and DIAP2, in the same insect cell line, SF-21 cells [12].
  • In addition, the diap2 anti-cell death gene is repressed in larval salivary glands as rpr and hid are induced, suggesting that the death of this tissue is under both positive and negative regulation [13].

Associations of Iap2 with chemical compounds


Regulatory relationships of Iap2

  • DIAP2 promotes cytoplasmic cleavage and nuclear translocation of the NF-kappaB homolog Relish, and this requires the DIAP2 RING domain [1].

Other interactions of Iap2

  • Inhibitors of ICE-family proteases p35 and crmA, as well as members of the iap class of genes, Op-iap and D-iap2, but not bcl-2 family members, blocked rpr-induced apoptosis [17].
  • Our preliminary data suggest that DIAP2 mediates DIAP1 degradation, suggesting a novel regulatory loop within the apoptotic pathway [18].
  • Interestingly, unlike other fly caspases, STRICA showed physical association with DIAP2, in cotransfection experiments [19].
  • These data suggest that DIAP1 and DIAP2 may be involved, possibly as negative regulators, in the Dpp signaling pathway, which leads to cell apoptosis [20].

Analytical, diagnostic and therapeutic context of Iap2

  • Sequence analysis of these alleles revealed that they were caused by single amino acid changes in the baculovirus IAP repeat domains of diap1, a domain implicated in binding REAPER, HID and GRIM [21].
  • Results from immunocytochemistry with two different ILP antisera showed cellular localizations in the nervous system and midgut that corroborated the existence of these expression patterns [22].


  1. The Drosophila inhibitor of apoptosis (IAP) DIAP2 is dispensable for cell survival, required for the innate immune response to gram-negative bacterial infection, and can be negatively regulated by the reaper/hid/grim family of IAP-binding apoptosis inducers. Huh, J.R., Foe, I., Muro, I., Chen, C.H., Seol, J.H., Yoo, S.J., Guo, M., Park, J.M., Hay, B.A. J. Biol. Chem. (2007) [Pubmed]
  2. The Drosophila Inhibitor of Apoptosis Protein DIAP2 Functions in Innate Immunity and Is Essential To Resist Gram-Negative Bacterial Infection. Leulier, F., Lhocine, N., Lemaitre, B., Meier, P. Mol. Cell. Biol. (2006) [Pubmed]
  3. Synthetic Smac peptide enhances the effect of etoposide-induced apoptosis in human glioblastoma cell lines. Mizukawa, K., Kawamura, A., Sasayama, T., Tanaka, K., Kamei, M., Sasaki, M., Kohmura, E. J. Neurooncol. (2006) [Pubmed]
  4. A mutational analysis of the baculovirus inhibitor of apoptosis Op-IAP. Vucic, D., Kaiser, W.J., Miller, L.K. J. Biol. Chem. (1998) [Pubmed]
  5. Destabilizing influences in apoptosis: sowing the seeds of IAP destruction. Martin, S.J. Cell (2002) [Pubmed]
  6. Structural basis of IAP recognition by Smac/DIABLO. Wu, G., Chai, J., Suber, T.L., Wu, J.W., Du, C., Wang, X., Shi, Y. Nature (2000) [Pubmed]
  7. A steroid-triggered transcriptional hierarchy controls salivary gland cell death during Drosophila metamorphosis. Jiang, C., Lamblin, A.F., Steller, H., Thummel, C.S. Mol. Cell (2000) [Pubmed]
  8. Inhibitor of apoptosis 2 and TAK1-binding protein are components of the Drosophila Imd pathway. Kleino, A., Valanne, S., Ulvila, J., Kallio, J., Myllymäki, H., Enwald, H., Stöven, S., Poidevin, M., Ueda, R., Hultmark, D., Lemaitre, B., Rämet, M. EMBO J. (2005) [Pubmed]
  9. Distinct cell killing properties of the Drosophila reaper, head involution defective, and grim genes. Wing, J.P., Zhou, L., Schwartz, L.M., Nambu, J.R. Cell Death Differ. (1998) [Pubmed]
  10. Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Martins, L.M., Morrison, A., Klupsch, K., Fedele, V., Moisoi, N., Teismann, P., Abuin, A., Grau, E., Geppert, M., Livi, G.P., Creasy, C.L., Martin, A., Hargreaves, I., Heales, S.J., Okada, H., Brandner, S., Schulz, J.B., Mak, T., Downward, J. Mol. Cell. Biol. (2004) [Pubmed]
  11. An RNA interference screen identifies Inhibitor of Apoptosis Protein 2 as a regulator of innate immune signalling in Drosophila. Gesellchen, V., Kuttenkeuler, D., Steckel, M., Pelte, N., Boutros, M. EMBO Rep. (2005) [Pubmed]
  12. Anti- and pro-apoptotic activities of baculovirus and Drosophila IAPs in an insect cell line. Harvey, A.J., Soliman, H., Kaiser, W.J., Miller, L.K. Cell Death Differ. (1997) [Pubmed]
  13. Steroid regulated programmed cell death during Drosophila metamorphosis. Jiang, C., Baehrecke, E.H., Thummel, C.S. Development (1997) [Pubmed]
  14. The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC. Muro, I., Hay, B.A., Clem, R.J. J. Biol. Chem. (2002) [Pubmed]
  15. A highly conserved arginine is critical for the functional folding of inhibitor of apoptosis (IAP) BIR domains. Luque, L.E., Grape, K.P., Junker, M. Biochemistry (2002) [Pubmed]
  16. Specification and development of the pars intercerebralis and pars lateralis, neuroendocrine command centers in the Drosophila brain. de Velasco, B., Erclik, T., Shy, D., Sclafani, J., Lipshitz, H., McInnes, R., Hartenstein, V. Dev. Biol. (2007) [Pubmed]
  17. Characterization of reaper- and FADD-induced apoptosis in a lepidopteran cell line. Vucic, D., Seshagiri, S., Miller, L.K. Mol. Cell. Biol. (1997) [Pubmed]
  18. Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways. Herman-Bachinsky, Y., Ryoo, H.D., Ciechanover, A., Gonen, H. Cell Death Differ. (2007) [Pubmed]
  19. STRICA, a novel Drosophila melanogaster caspase with an unusual serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2. Doumanis, J., Quinn, L., Richardson, H., Kumar, S. Cell Death Differ. (2001) [Pubmed]
  20. Interaction of Drosophila inhibitors of apoptosis with thick veins, a type I serine/threonine kinase receptor for decapentaplegic. Oeda, E., Oka, Y., Miyazono, K., Kawabata, M. J. Biol. Chem. (1998) [Pubmed]
  21. Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function. Goyal, L., McCall, K., Agapite, J., Hartwieg, E., Steller, H. EMBO J. (2000) [Pubmed]
  22. Molecular characterization of insulin-like peptides in the yellow fever mosquito, Aedes aegypti: Expression, cellular localization, and phylogeny. Riehle, M.A., Fan, Y., Cao, C., Brown, M.R. Peptides (2006) [Pubmed]
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