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Janeway CA Jr, Travers P, Walport M, et al. Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001.

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Immunobiology: The Immune System in Health and Disease. 5th edition.

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Figure 1. A comparison of the Drosophila and mammalian Toll signaling pathways.

Figure 1A comparison of the Drosophila and mammalian Toll signaling pathways

The components of the mammalian Toll-like receptor signaling pathway that culminates in the activation of NFκB have direct parallels in the components of the signaling pathway from the Toll receptor of Drosophila. The intracellular domain of the Toll-like receptors interacts with a homologous domain in the adaptor protein MyD88. A similar interaction occurs between the intracellular domain of Toll and dMyD88. The next step in both signaling pathways occurs via the interaction of death domains, between MyD88 and IRAK in the mammalian cells and between dMyD88 and Pelle in Drosophila. Both IRAK and Pelle are serine kinases. At this point the mammalian signaling pathway passes through an adaptor, TRAF6, which is activated by IRAK and in turn activates IKK. IKK phosphorylates the inhibitor of NFκB, IκB, targeting it for degradation and releasing the active dimeric transcription factor, NFκB. In Drosophila, homologues of MyD88, TRAF6, and of a kinase that is homologous to IKK that phosphorylates the Drosophila IκB homologue Cactus are found. Moreover, the terminal parts of the pathway are also homologous between Drosophila and mammals; phosphorylation of Cactus initiates its degradation and the release of the Dif/Relish dimer, which is a transcription factor and homologue of NFκB.

From: Evolution of the innate immune system

Copyright © 2001, Garland Science.

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