THE HUMAN INTERLEUKIN-11 RECEPTOR-ALPHA GENE (IL11RA) - GENOMIC ORGANIZATION AND CHROMOSOME MAPPING

The high-affinity receptor for interleukin-ll (IL-11) is composed of t wo subunits, IL-11 receptor alpha chain (IL-11R alpha) and gp130, the common subunit of the interleukin-6 (IL-6), ciliary neurotrophic facto r (CNTF), leukemia inhibitory factor, and oncostatin M receptors. The IL-11 receptor-specific alpha chain shares homologies with the alpha c hain of the CNTF and IL-6 receptors. We isolated and characterized gen omic DNA clones encompassing the entire coding sequence of the IL-11R alpha cDNA. The exon-intron organization of the IL-11R gene (HGMW-appr oved symbol IL11RA) is consistent with the predicted structure of the different domains of the IL-11R alpha protein, confirming evolutionary conservation at the level of gene organization among the hematopoieti c cytokine receptor family. The IL-IIR gene has been assigned to chrom osome 9 band p13 by in situ hybridization using human IL-11R alpha cDN A as a probe. The fact that the ciliary neurotrophic factor (CNTFR) ge ne has recently been localized on this same band and the conserved gen omic structure between IL-IIR and CNTFR suggest that they may have evo lved from a common ancestor. (C) 1996 Academic Press, Inc.