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Gene Review

Rel  -  Relish

Drosophila melanogaster

Synonyms: CG11992, Dmel\CG11992, NF-kappaB, NFkappaB, Nuclear factor NF-kappa-B p110 subunit, ...
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Disease relevance of Rel


High impact information on Rel

  • A novel Rel-containing gene in Drosophila, Dif (dorsal-related immunity factor), provides a potential link between these seemingly disparate processes [4].
  • Both depend on regulatory factors containing rel domains (dorsal and NF-kappa B) that are controlled at the level of nuclear transport [4].
  • These results provide direct evidence for the role of phosphorylation in the in vivo regulation of a rel-like transcription factor [5].
  • The dl protein recognizes a sequence motif similar to that of the mammalian transcriptional activator NF-kappa B, which was shown to contain extensive homology with dl and the oncoprotein rel [6].
  • In response to infection, two Rel proteins, Dif and Dorsal, translocate from the cytoplasm to the nuclei of larval fat-body cells [7].

Biological context of Rel

  • We have identified the first endogenous targets of the mbo nuclear import pathway in the Rel proteins Dorsal and Dif [8].
  • These results illustrate how the formation of Rel protein dimers differentially regulate target gene expression [9].
  • NF-kappaB/Rel family proteins regulate genes that are critical for many cellular processes including apoptosis, inflammation, immune response, and development [9].
  • NF-kappaB/Rel proteins function as homodimers or heterodimers, which recognize specific DNA sequences within target promoters [9].
  • Innate immunity and hematopoiesis are regulated by analogous Rel/NF-kappaB-family pathways in mammals [10].

Anatomical context of Rel

  • We examined the activity of different Drosophila Rel-related proteins in modulating Drosophila immunity genes by expressing the Rel proteins in stably transfected cell lines [9].
  • The lesswright mutation activates Rel-related proteins, leading to overproduction of larval hemocytes in Drosophila melanogaster [11].
  • Here we show that mutants that lack the Drosophila Rel/NF-kappaB proteins Dorsal and Dif have very few blood cells, are constitutively infected by opportunistic microbes, and die from infection as larvae [12].
  • We show that two of the three Drosophila Rel/NF-kappa B genes are expressed in doomed salivary glands and that one family member, Dif, is induced in a stage-specific manner immediately before the onset of programmed cell death [13].
  • In Drosophila, a coordinate interplay between the Rel transcription factor Dorsal and the basic Helix-Loop-Helix transcription factor Twist initiates mesoderm formation by activating the zygotic expression of mesoderm-determining genes [14].

Associations of Rel with chemical compounds


Regulatory relationships of Rel

  • The current model of immune activation in Drosophila melanogaster suggests that fungi and Gram-positive (G(+)) bacteria activate the Toll/Dif pathway and that Gram-negative (G(-)) bacteria activate the Imd/Relish pathway [1].
  • Signaling by Drosophila Toll pathway activates two Rel/NF-kappaB transcription factors, Dorsal (Dl) and Dorsal-related immune factor (Dif) [19].
  • This result suggests a functional redundancy between both Rel proteins in the control of drosomycin gene expression in the larvae of Drosophila [20].
  • Like the Toll pathway, the IMD pathway regulates antimicrobial peptide gene expression via a Rel/nuclear factor (NF)-kappaB-like transcription factor [21].
  • The interaction of Sp1 with NF-kappaB sites thus provides a means to keep an elevated basal expression of NF-kappaB-dependent genes in the absence of activated nuclear NF-kappaB/Rel [22].

Other interactions of Rel

  • In addition, we find that the activated DmIKK complex, as well as recombinant DmIKKbeta, can phosphorylate Relish in vitro [23].
  • Although the R1 motif was required for Rel protein-mediated CecA1 expression in cotransfection experiments, our data argue against it being a direct target for the Drosophila Rel proteins [24].
  • Various fungi stimulated antimicrobial peptides through at least two different pathways requiring Relish and/or Dif [1].
  • Induction of Attacin A by Geotrichum candidum required Relish, whereas activation by Beauvaria bassiana required Dif, suggesting that the Drosophila immune system can distinguish between at least these two fungi [1].
  • Thus, a yet to be identified IkappaB kinase complex must be required for Rel protein activation via the Toll signaling pathway [23].

Analytical, diagnostic and therapeutic context of Rel

  • PCR and Southern blot hybridization analyses show that these three transcripts originated from the same large inducible mRNA encoded by a single Relish gene [2].
  • Molecular cloning and characterization of SRAM, a novel insect rel/ankyrin-family protein present in nuclei [25].
  • A cDNA encoding a Rel/NF-kappaB homologue was cloned from a beetle, Allomyrina dichotoma, by reverse transcriptase-polymerase chain reactions (RT-PCR) taking advantage of the conserved Rel homology domain (RHD) to synthesize primers [26].
  • However, in situ hybridization of rat tissues demonstrated more restricted expression of Rel-N1 mRNA within a subset of neurons of the hippocampus, cortex, and other regions of the gray matter, but not in glial cells or white matter [27].
  • Electrophoretic mobility shift assay further confirmed a strong interaction of the limulus kappaB motif with Rel proteins [18].


  1. Differential activation of the NF-kappaB-like factors Relish and Dif in Drosophila melanogaster by fungi and Gram-positive bacteria. Hedengren-Olcott, M., Olcott, M.C., Mooney, D.T., Ekengren, S., Geller, B.L., Taylor, B.J. J. Biol. Chem. (2004) [Pubmed]
  2. Characterization of three alternatively spliced isoforms of the Rel/NF-kappa B transcription factor Relish from the mosquito Aedes aegypti. Shin, S.W., Kokoza, V., Ahmed, A., Raikhel, A.S. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Role of Drosophila IKK gamma in a toll-independent antibacterial immune response. Rutschmann, S., Jung, A.C., Zhou, R., Silverman, N., Hoffmann, J.A., Ferrandon, D. Nat. Immunol. (2000) [Pubmed]
  4. Dif, a dorsal-related gene that mediates an immune response in Drosophila. Ip, Y.T., Reach, M., Engstrom, Y., Kadalayil, L., Cai, H., González-Crespo, S., Tatei, K., Levine, M. Cell (1993) [Pubmed]
  5. pelle encodes a protein kinase required to establish dorsoventral polarity in the Drosophila embryo. Shelton, C.A., Wasserman, S.A. Cell (1993) [Pubmed]
  6. The dorsal morphogen is a sequence-specific DNA-binding protein that interacts with a long-range repression element in Drosophila. Ip, Y.T., Kraut, R., Levine, M., Rushlow, C.A. Cell (1991) [Pubmed]
  7. Regulated nuclear import of Rel proteins in the Drosophila immune response. Wu, L.P., Anderson, K.V. Nature (1998) [Pubmed]
  8. members only encodes a Drosophila nucleoporin required for rel protein import and immune response activation. Uv, A.E., Roth, P., Xylourgidis, N., Wickberg, A., Cantera, R., Samakovlis, C. Genes Dev. (2000) [Pubmed]
  9. Interaction and specificity of Rel-related proteins in regulating Drosophila immunity gene expression. Han, Z.S., Ip, Y.T. J. Biol. Chem. (1999) [Pubmed]
  10. Control of development and immunity by rel transcription factors in Drosophila. Govind, S. Oncogene (1999) [Pubmed]
  11. The lesswright mutation activates Rel-related proteins, leading to overproduction of larval hemocytes in Drosophila melanogaster. Huang, L., Ohsako, S., Tanda, S. Dev. Biol. (2005) [Pubmed]
  12. Rel/NF-{kappa}B double mutants reveal that cellular immunity is central to Drosophila host defense. Matova, N., Anderson, K.V. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  13. AP-1, but not NF-kappa B, is required for efficient steroid-triggered cell death in Drosophila. Lehmann, M., Jiang, C., Ip, Y.T., Thummel, C.S. Cell Death Differ. (2002) [Pubmed]
  14. Mesoderm-determining transcription in Drosophila is alleviated by mutations in TAF(II)60 and TAF(II)110. Pham, A.D., Müller, S., Sauer, F. Mech. Dev. (1999) [Pubmed]
  15. 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]
  16. Caspase-mediated processing of the Drosophila NF-kappaB factor Relish. Stoven, S., Silverman, N., Junell, A., Hedengren-Olcott, M., Erturk, D., Engstrom, Y., Maniatis, T., Hultmark, D. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  17. A protein kinase-A recognition sequence is structurally linked to transformation by p59v-rel and cytoplasmic retention of p68c-rel. Mosialos, G., Hamer, P., Capobianco, A.J., Laursen, R.A., Gilmore, T.D. Mol. Cell. Biol. (1991) [Pubmed]
  18. Transcriptional regulation of limulus factor C: repression of an NFkappaB motif modulates its responsiveness to bacterial lipopolysaccharide. Wang, L., Ho, B., Ding, J.L. J. Biol. Chem. (2003) [Pubmed]
  19. REL1, a homologue of Drosophila dorsal, regulates toll antifungal immune pathway in the female mosquito Aedes aegypti. Shin, S.W., Kokoza, V., Bian, G., Cheon, H.M., Kim, Y.J., Raikhel, A.S. J. Biol. Chem. (2005) [Pubmed]
  20. A mosaic analysis in Drosophila fat body cells of the control of antimicrobial peptide genes by the Rel proteins Dorsal and DIF. Manfruelli, P., Reichhart, J.M., Steward, R., Hoffmann, J.A., Lemaitre, B. EMBO J. (1999) [Pubmed]
  21. Drosophila immunity: two paths to NF-kappaB. Khush, R.S., Leulier, F., Lemaitre, B. Trends Immunol. (2001) [Pubmed]
  22. Functional interference of Sp1 and NF-kappaB through the same DNA binding site. Hirano, F., Tanaka, H., Hirano, Y., Hiramoto, M., Handa, H., Makino, I., Scheidereit, C. Mol. Cell. Biol. (1998) [Pubmed]
  23. 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]
  24. Functional characterization of a novel promoter element required for an innate immune response in Drosophila. Uvell, H., Engström, Y. Mol. Cell. Biol. (2003) [Pubmed]
  25. Molecular cloning and characterization of SRAM, a novel insect rel/ankyrin-family protein present in nuclei. Shiraishi, H., Kobayashi, A., Sakamoto, Y., Nonaka, T., Mitsui, Y., Aozasa, N., Kubo, T., Natori, S. J. Biochem. (2000) [Pubmed]
  26. Characterization of a homologue of the Rel/NF-kappaB transcription factor from a beetle, Allomyrina dichotoma. Sagisaka, A., Tanaka, H., Furukawa, S., Yamakawa, M. Biochim. Biophys. Acta (2004) [Pubmed]
  27. Mammalian homologs of Drosophila ELAV localized to a neuronal subset can bind in vitro to the 3' UTR of mRNA encoding the Id transcriptional repressor. King, P.H., Levine, T.D., Fremeau, R.T., Keene, J.D. J. Neurosci. (1994) [Pubmed]
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