Interleukin 13 (IL-13) has been shown to play a critical role in the allergic diseases and bronchial asthma. However, signal transduction mechanisms for IL-13 receptor complex is still completely not clear. To investigate its signal transduction pathways, we have cloned new IL-13Ralpha' binding protein by yeast tri-hybrid system and designated it interleukin 13 receptor binding protein 1 (IL-I3RBP1). IL-13RBP1 cDNA is 2370 bp in length with open reading frame predicted to encode a protein of 625 amino acids. MOTIF search analysis revealed that IL-13RBP1 cDNA contains a myosin heavy chain like sequence in the N terminal end, nuclear localization signal in the middle part and coiled-coil region in C terminal end. We next examined mRNA expression in human tissues by Northern analysis and found that two different sizes (4.4 and 2.4 kb) of IL13RBP1 transcripts were present in most tissues. In addition, testis contained an additional 3 types of transcripts of -2.7 kb. Database searches utilizing BLAST and FASTA programs failed to identify any mammalian proteins having significant sequence similarities to IL13RBP1. However, C. elegans and D. melanogaster proteins of unknown function share -20% similarity to IL-13RBP1. IL13RBP1 may provide a novel mechanism in IL-13R signal transduction pathways.
|Issue number||11 PART II|
|Publication status||Published - 2000|
ASJC Scopus subject areas
- Cell Biology