T6BP, a TRAF6-interacting protein involved in IL-1 signaling.

We report the identification of a TRAF-interacting protein, T6BP, that specifically associates with TRAF6. This interaction occurs between the coiled-coil region of T6BP and the N-terminal ring finger and zinc finger domains of TRAF6. IL-1, but not tumor necrosis factor, induces TRAF6-T6BP complex formation in a ligand-dependent manner. Formation of ...
the TRAF6-T6BP complex depends on the presence of the IL-1 receptor-associated kinase (IRAK). After IL-1 stimulation, TRAF6 can exist in two separate complexes, TRAF6-IRAK or TRAF6-T6BP, but IRAK is not present in TRAF6-T6BP complexes. T6BP does not seem to play a direct role in activation of IkappaB kinases or Jun N-terminal kinase.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Carrier Proteins, Cell Line, DNA, Complementary, Dimerization, Enzyme Activation, Humans, Interleukin-1, Interleukin-1 Receptor-Associated Kinases, Intracellular Signaling Peptides and Proteins, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase Kinase 1, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Molecular Weight, NF-kappa B, Neoplasm Proteins, Protein Binding, Protein Kinases, Protein-Serine-Threonine Kinases, Proteins, Sequence Alignment, Signal Transduction, Substrate Specificity, TNF Receptor-Associated Factor 6, Transfection, Two-Hybrid System Techniques, Zinc Fingers
Proc. Natl. Acad. Sci. U.S.A.
Date: Aug. 15, 2000
Download Curated Data For This Publication
11091
Switch View:
  • Interactions 5