Journal article

Publication year: 1999

Pages: 81-85

Journal: FEBS Letters

Volume number: 448

Issue number: 1

ISSN: 0014-5793

DOI Link: https://doi.org/10.1016/S0014-5793(99)00322-1

Publisher: Wiley

Abstract: 
Interleukin-1 (IL-1) stimulates the association of the IL-1 receptor-associated protein kinase (IRAK) with the heterodimer of IL-1RI and IL-1RAcP via the adapter protein MyD88. In the receptor complex IRAK becomes heavily phosphorylated and concomitantly activated. Here we show that overexpression of a kinase-inactive mutant of IRAK (K239S) inhibits neither IL-1-stimulated activation of the transcription factor NF-kappa B, nor that of the c-Jun N-terminal kinase nor IL-2 production in murine EL-4 cells, but enhances these effects in a manner comparable to wild type IRAK. This strongly suggests that the intrinsic kinase activity is not required for downstream signaling via IRAK. (C) 1999 Federation of European Biochemical Societies.

Harvard Citation style: Knop, J. and Martin, M. (1999) Effects of IL-1 receptor-associated kinase (IRAK) expression on IL-1 signaling are independent of its kinase activity, FEBS Letters, 448(1), pp. 81-85. https://doi.org/10.1016/S0014-5793(99)00322-1

APA Citation style: Knop, J., & Martin, M. (1999). Effects of IL-1 receptor-associated kinase (IRAK) expression on IL-1 signaling are independent of its kinase activity. FEBS Letters. 448(1), 81-85. https://doi.org/10.1016/S0014-5793(99)00322-1