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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

Authors

  • Ling L
  • Goeddel DV

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Data

August 15, 2000

Associated Grants

None

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