The death domain of IRAK-1: an oligomerization domain mediating interactions with MyD88, Tollip, IRAK-1, and IRAK-4.

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.
Mesh Terms:
Amino Acid Sequence, Cell Line, Tumor, Humans, Interleukin-1 Receptor-Associated Kinases, Intracellular Signaling Peptides and Proteins, Myeloid Differentiation Factor 88, Protein Structure, Tertiary, Receptors, Death Domain, Signal Transduction, Threonine, Thymoma
Biochem. Biophys. Res. Commun.
Date: Mar. 23, 2007
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