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RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis.

Signaling through the CD95/Fas/APO-1 death receptor plays a critical role in the homeostasis of the immune system. RICK, a novel protein kinase that regulates CD95-mediated apoptosis was identified and characterized. RICK is composed of an N-terminal serine-threonine kinase catalytic domain and a C-terminal region containing a caspase-recruitment domain. RICK physically interacts with CLARP, a caspase-like molecule known to bind to Fas-associated protein with death domain (FADD) and caspase-8. Expression of RICK promoted the activation of caspase-8 and potentiated apoptosis induced by Fas ligand, FADD, CLARP, and caspase-8. Deletion mutant analysis revealed that both the kinase domain and caspase-recruitment domain were required for RICK to promote apoptosis. Significantly, expression of a RICK mutant in which the lysine of the putative ATP-binding site at position 38 was replaced by a methionine functioned as an inhibitor of CD95-mediated apoptosis. Thus, RICK represents a novel kinase that may regulate apoptosis induced by the CD95/Fas receptor pathway.

Pubmed ID: 9575181


  • Inohara N
  • del Peso L
  • Koseki T
  • Chen S
  • Núñez G


The Journal of biological chemistry

Publication Data

May 15, 1998

Associated Grants

  • Agency: NCI NIH HHS, Id: CA-64556

Mesh Terms

  • Adenosine Triphosphate
  • Amino Acid Sequence
  • Antigens, CD95
  • Apoptosis
  • Binding Sites
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • Cysteine Endopeptidases
  • DNA, Complementary
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Molecular Sequence Data
  • Mutagenesis
  • Protein Binding
  • Protein Kinases
  • Proteins
  • Receptor-Interacting Protein Serine-Threonine Kinase 2
  • Sequence Deletion
  • Sequence Homology, Amino Acid