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The death domain kinase RIP mediates the TNF-induced NF-kappaB signal.

The death domain serine/threonine kinase RIP interacts with the death receptors Fas and tumor necrosis receptor 1 (TNFR1). In vitro, RIP stimulates apoptosis, SAPK/JNK, and NF-kappaB activation. To define the physiologic role(s) that RIP plays in regulating apoptosis in vivo, we introduced a rip null mutation in mice through homologous recombination. RIP-deficient mice appear normal at birth but fail to thrive, displaying extensive apoptosis in both the lymphoid and adipose tissue and dying at 1-3 days of age. In contrast to a normal thymic anti-Fas response, rip-/- cells are highly sensitive to TNFalpha-induced cell death. Sensitivity to TNFalpha-mediated cell death in rip-/- cells is accompanied by a failure to activate the transcription factor NF-kappaB.

Pubmed ID: 9529147

Authors

  • Kelliher MA
  • Grimm S
  • Ishida Y
  • Kuo F
  • Stanger BZ
  • Leder P

Journal

Immunity

Publication Data

March 16, 1998

Associated Grants

None

Mesh Terms

  • Adipose Tissue
  • Animals
  • Antigens, CD95
  • Apoptosis
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cytokines
  • Failure to Thrive
  • Genes, Lethal
  • JNK Mitogen-Activated Protein Kinases
  • Lymphoid Tissue
  • Mice
  • Mice, Mutant Strains
  • Mitogen-Activated Protein Kinases
  • NF-kappa B
  • Protein-Serine-Threonine Kinases
  • Proteins
  • Receptor-Interacting Protein Serine-Threonine Kinases
  • Tumor Necrosis Factor-alpha