Journal article

Publication year: 2007

Pages: 1089-1094

Journal: Biochemical and Biophysical Research Communications

Volume number: 354

Issue number: 4

ISSN: 0006-291X

DOI Link: https://doi.org/10.1016/j.bbrc.2007.01.104

Publisher: Elsevier

Abstract: 
Ligand binding in the Toll-like/interleukin-1 receptor family results in the recruitment of an intracellular signaling complex. IRAK-1, which is centrally involved in this complex, is able to homo-oligomerize and to bind to Tollip and the adapters MyD88 and IRAK-4. The interactions of IRAK-1 with MyD88 or Tollip are mediated by the N-terminal part of IRAK-1, containing the death domain with the highly conserved threonine at position 66 (T66). Mutation of this amino acid into alanine or aspartic acid stabilized binding to MyD88, Tollip, and IRAK-4, allowing the definitive experimental proof, that all these interactions are mediated by the death domain of IRAK-1. Homo-oligomerization of IRAK-1, which is mediated by the death domain too, is not affected by mutation of T66. Finally, mutation of IRAK-1 at T66 not only allowed stable binding to the signaling adapters, but also enhanced its signaling capacity. (c) 2007 Elsevier Inc. All rights reserved.

Harvard Citation style: Neumann, D., Kollewe, C., Resch, K. and Martin, M. (2007) The death domain of IRAK-1: An oligomerization domain mediating interactions with MyD88, Tollip, IRAK-1, and IRAK-4, Biochemical and Biophysical Research Communications, 354(4), pp. 1089-1094. https://doi.org/10.1016/j.bbrc.2007.01.104

APA Citation style: Neumann, D., Kollewe, C., Resch, K., & Martin, M. (2007). The death domain of IRAK-1: An oligomerization domain mediating interactions with MyD88, Tollip, IRAK-1, and IRAK-4. Biochemical and Biophysical Research Communications. 354(4), 1089-1094. https://doi.org/10.1016/j.bbrc.2007.01.104