Journal article

Publication year: 2008

Pages: 807-813

Journal: Journal of Leukocyte Biology

Volume number: 84

Issue number: 3

ISSN: 0741-5400

DOI Link: https://doi.org/10.1189/jlb.0507290

Publisher: Oxford University Press

Abstract: 
Ligand binding in the TLR/IL-1R family results in the transient formation of an intracellular signaling complex, which contains, amongst others, the serine/ threonine- specific kinase IL- 1R- associated kinase 1 ( IRAK- 1). Concomitantly, the kinase function of IRAK- 1 becomes activated, resulting in massive autophosphorylation and finally in the dissociation of the initially constituted signaling complex. The death domain ( DD) of IRAK- 1 mediates the interaction with other molecules of the signaling complex, e. g., the adaptor MyD88, the silencer Tollip, and the activator kinase IRAK- 4. The conserved threonine at position 66 ( T66), located within the DD, is a putative autophosphorylation target site. Here, we provide evidence that T66 critically impacts the secondary structure of the IRAK- 1 DD. Thereby, it ensures the transient manner of interactions between IRAK- 1 and the other signaling molecules. This essential role, however, is not regulated by phosphorylation of T66 itself.

Harvard Citation style: Neumann, D., Kollewe, C., Pich, A., Cao, P., Resch, K. and Martin, M. (2008) Threonine 66 in the death domain of IRAK-1 is critical for interaction with signaling molecules but is not a target site for autophosphorylation, Journal of Leukocyte Biology, 84(3), pp. 807-813. https://doi.org/10.1189/jlb.0507290

APA Citation style: Neumann, D., Kollewe, C., Pich, A., Cao, P., Resch, K., & Martin, M. (2008). Threonine 66 in the death domain of IRAK-1 is critical for interaction with signaling molecules but is not a target site for autophosphorylation. Journal of Leukocyte Biology. 84(3), 807-813. https://doi.org/10.1189/jlb.0507290