T1/ST2 Signaling Establishes It as a Member of an Expanding Interleukin-1 Receptor Family
作者： Jennifer L. Mitcham , Patricia Parnet , Timothy P. Bonnert , Kirsten E. Garka , Mary J. Gerhart
关键词: Genetics 、 Peptide sequence 、 Interleukin-1 Receptor-Like 1 Protein 、 Homology (biology) 、 Protein superfamily 、 Signal transduction 、 Consensus sequence 、 Interleukin-1 receptor family 、 Membrane protein 、 Biology
摘要: Through data base searches, we have discovered new proteins that share homology with the signaling domain of type I interleukin-1 receptor (IL-1RI): human "randomly sequenced cDNA 786" (rsc786), murine MyD88, and two partial Drosophila open reading frames, MstProx STSDm2245. Comparisons between these known IL-1RI homologous such as Toll, 18-Wheeler, T1/ST2 revealed six clusters amino acid similarity. We tested hypothesis sequence similarity three mammalian family members might indicate functional Chimeric receptors expressing putative domains T1/ST2, rsc786 were assayed by separate IL-1 responsive assays, NF-kappaB, phosphorylation an epidermal growth factor peptide, interleukin 8 promoter-controlled reporter construct, for their ability to transduce IL-1-stimulated signal. All assays positive in response chimera, while MyD88 chimeras failed respond. These indicates a well.
sci-hub.se 参考文章(39)
G. Bergers, A. Reikerstorfer, S. Braselmann, P. Graninger, M. Busslinger, Alternative promoter usage of the Fos-responsive gene Fit-1 generates mRNA isoforms coding for either secreted or membrane-bound proteins related to the IL-1 receptor. The EMBO Journal. ,vol. 13, pp. 1176- 1188 ,(1994) , 10.1002/J.1460-2075.1994.TB06367.X
D A Liebermann, K A Lord, B Hoffman-Liebermann, Nucleotide sequence and expression of a cDNA encoding MyD88, a novel myeloid differentiation primary response gene induced by IL6. Oncogene. ,vol. 5, pp. 1095- 1097 ,(1990)
T.A. Bird, P.R. Sleath, P.C. deRoos, S.K. Dower, G.D. Virca, Interleukin-1 represents a new modality for the activation of extracellular signal-regulated kinases/microtubule-associated protein-2 kinases. Journal of Biological Chemistry. ,vol. 266, pp. 22661- 22670 ,(1991) , 10.1016/S0021-9258(18)54621-4
G R Guy, X Cao, S P Chua, Y H Tan, Okadaic acid mimics multiple changes in early protein phosphorylation and gene expression induced by tumor necrosis factor or interleukin-1. Journal of Biological Chemistry. ,vol. 267, pp. 1846- 1852 ,(1992) , 10.1016/S0021-9258(18)46024-3
J. Ostrowski, J.E. Sims, C.H. Sibley, M.A. Valentine, S.K. Dower, K.E. Meier, K. Bomsztyk, A serine/threonine kinase activity is closely associated with a 65-kDa phosphoprotein specifically recognized by the kappa B enhancer element. Journal of Biological Chemistry. ,vol. 266, pp. 12722- 12733 ,(1991) , 10.1016/S0021-9258(18)98959-3
Charles A. Dinarello, The interleukin-1 family: 10 years of discovery. The FASEB Journal. ,vol. 8, pp. 1314- 1325 ,(1994) , 10.1096/FASEBJ.8.15.8001745
K. Leung, J.C. Betts, L. Xu, G.J. Nabel, The cytoplasmic domain of the interleukin-1 receptor is required for nuclear factor-kappa B signal transduction. Journal of Biological Chemistry. ,vol. 269, pp. 1579- 1582 ,(1994) , 10.1016/S0021-9258(17)42061-8
A Heguy, C T Baldari, G Macchia, J L Telford, M Melli, Amino acids conserved in interleukin-1 receptors (IL-1Rs) and the Drosophila toll protein are essential for IL-1R signal transduction. Journal of Biological Chemistry. ,vol. 267, pp. 2605- 2609 ,(1992) , 10.1016/S0021-9258(18)45924-8
CA Dinarello, Interleukin-1 and interleukin-1 antagonism. Blood. ,vol. 77, pp. 1627- 1652 ,(1991) , 10.1182/BLOOD.V77.8.1627.1627
T A Bird, J M Kyriakis, L Tyshler, M Gayle, A Milne, G D Virca, Interleukin-1 activates p54 mitogen-activated protein (MAP) kinase/stress-activated protein kinase by a pathway that is independent of p21ras, Raf-1, and MAP kinase kinase. Journal of Biological Chemistry. ,vol. 269, pp. 31836- 31844 ,(1994) , 10.1016/S0021-9258(18)31771-X