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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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T1/ST2 signaling establishes it as a member of an expanding interleukin-1 receptor family.

Through data base searches, we have discovered new proteins that share homology with the signaling domain of the type I interleukin-1 receptor (IL-1RI): human "randomly sequenced cDNA 786" (rsc786), murine MyD88, and two partial Drosophila open reading frames, MstProx and STSDm2245. Comparisons between these new proteins and known IL-1RI homologous proteins such as Toll, 18-Wheeler, and T1/ST2 revealed six clusters of amino acid similarity. We tested the hypothesis that sequence similarity between the signaling domain of IL-1RI and the three mammalian family members might indicate functional similarity. Chimeric IL-1RI receptors expressing the putative signaling domains of T1/ST2, MyD88, and rsc786 were assayed by three separate IL-1 responsive assays, NF-kappaB, phosphorylation of an epidermal growth factor receptor peptide, and an interleukin 8 promoter-controlled reporter construct, for their ability to transduce an IL-1-stimulated signal. All three assays were positive in response to the T1/ST2 chimera, while the MyD88 and rsc786 chimeras failed to respond. These data indicate that the sequence homology between IL-1RI and T1/ST2 indicates a functional homology as well.[1]

References

  1. T1/ST2 signaling establishes it as a member of an expanding interleukin-1 receptor family. Mitcham, J.L., Parnet, P., Bonnert, T.P., Garka, K.E., Gerhart, M.J., Slack, J.L., Gayle, M.A., Dower, S.K., Sims, J.E. J. Biol. Chem. (1996) [Pubmed]
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