Journalartikel

Jahr der Veröffentlichung: 1999

Seiten: 81-85

Zeitschrift: FEBS Letters

Bandnummer: 448

Heftnummer: 1

ISSN: 0014-5793

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

Verlag: 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-Zitierstil: 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-Zitierstil: 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