• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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


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



Publication Data

March 16, 1998

Associated Grants


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