Inhibition of fas death signals by FLIPs

Curr Opin Immunol. 1998 Oct;10(5):552-8. doi: 10.1016/s0952-7915(98)80223-9.


The death receptor Fas is a member of the tumor necrosis factor receptor family; upon interaction with its ligand it efficiently activates caspases and induces apoptosis. Despite abundant Fas surface expression, however, Fas death-signals are frequently interrupted. Many viruses express antiapoptotic proteins, including caspase inhibitors, Bcl-2 homologues and death-effector-domain-containing proteins that are termed FLIPs (FLICE [Fas-associated death-domain-like IL-1beta-converting enzyme]-inhibitory proteins). Cellular homologues of these inhibitors have been identified. Cellular FLIPs structurally resemble caspase-8 except that they lack proteolytic activity. FLIPs are highly expressed in tumor cells, T lymphocytes and healthy, but not injured, myocytes; this suggests a critical role of FLIPs as endogenous modulators of apoptosis.

Publication types

  • Review

MeSH terms

  • Animals
  • Apoptosis*
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • Carrier Proteins / physiology*
  • Caspase Inhibitors
  • Caspases / physiology
  • Fas Ligand Protein
  • Humans
  • Intracellular Signaling Peptides and Proteins*
  • Membrane Glycoproteins / physiology
  • Proto-Oncogene Proteins c-bcl-2 / physiology
  • fas Receptor / physiology*


  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • CFLAR protein, human
  • Carrier Proteins
  • Caspase Inhibitors
  • FASLG protein, human
  • Fas Ligand Protein
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • Proto-Oncogene Proteins c-bcl-2
  • fas Receptor
  • Caspases