Chromosomal localization of TIL, a gene encoding a protein related to the Drosophila transmembrane receptor toll, to human chromosome 4p14

• Published in: Genomics (San Diego, Calif.) Calif.), 1996-03, Vol.32 (3), p.486-488
• Main Authors: TAGUCHI, T, MITCHAM, J. L, DOWER, S. K, SIMS, J. E, TESTA, J. R
• Format: Article
• Language: English
• Subjects: Animals; Biological and medical sciences; Chromosome Mapping; Chromosomes, Human, Pair 4; Classical genetics, quantitative genetics, hybrids; Drosophila; Drosophila melanogaster; Drosophila Proteins; Fundamental and applied biological sciences. Psychology; Genetics of eukaryotes. Biological and molecular evolution; Human; Humans; In Situ Hybridization, Fluorescence; Insect Hormones - genetics; Membrane Glycoproteins - genetics; Receptors, Cell Surface - genetics; Receptors, Interleukin-1 - genetics; Toll-Like Receptors
• ISSN: 0888-7543; 1089-8646
• DOI: 10.1006/geno.1996.0150

The Drosophila transmembrane receptor Toll and the mammalian interleukin-1 (IL-1) receptor are known to share similarities in both amino-acid sequence and function. Toll is involved in establishing the dorsal/ventral axis in the developing Drosophila embryo. In response to its ligand, spatzle, Toll causes activation of DNA binding by the dorsal gene product, a homolog of NF Kappa B. IL-1 is a prime mediator of inflammatory responses. One of the consequences of IL-1 stimulation of cells is activation of DNA binding by the transcription factor NF Kappa B. This functional similarity reflects a high degree of sequence conservation in the cytoplasmic domains of the IL-1 receptor and Toll proteins. However, the sequence conservation does not extend to the ligand-binding portions of the molecules. The extracellular domain of Toll consists in large part of a series of leucine-rich repeats, whereas that of the IL-1 receptor comprises three immunoglobulin-like domains. Not surprisingly, the ligands for these receptors, spatzle and IL-1, show no sequence similarity.