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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.

Pubmed ID: 10920205 RIS Download

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

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