Recruitment of TRADD, FADD, and caspase 8 to double-stranded RNA-triggered death inducing signaling complexes (dsRNA-DISCs)

Apoptosis. 2005 Jan;10(1):167-76. doi: 10.1007/s10495-005-6071-x.

Abstract

Rapid elimination of virus-infected cells by apoptosis is an efficient anti-viral strategy. Double-stranded RNA (dsRNA), a viral product, is potently and rapidly apoptogenic in susceptible cells. Caspase 8 plays an important role in the dsRNA-induced apoptosis; however, the mechanisms of caspase 8 activation in response to dsRNA are unknown. We demonstrate here that, in HeLa cells, the dsRNA-triggered activation of caspase 8 is independent of ongoing proteins synthesis (and is, therefore, independent of changes in pro- and anti-apoptotic gene expression) and involves the formation of multiprotein dsRNA-triggered death inducing signaling complexes (dsRNA-DISCs). DsRNA-DISCs contain FADD, TRADD, and caspase 8; however, several experimental approaches suggest that death ligands and death receptors (such as Fas/Apo1 and DR4/Apo2) are not involved in the formation of dsRNA-DISCs.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism*
  • Apoptosis*
  • Caspase 8
  • Caspases / metabolism*
  • Death Domain Receptor Signaling Adaptor Proteins
  • Fas-Associated Death Domain Protein
  • HeLa Cells
  • Humans
  • RNA, Double-Stranded / metabolism*
  • Receptors, Tumor Necrosis Factor / metabolism*
  • Signal Transduction*
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / metabolism*

Substances

  • Adaptor Proteins, Signal Transducing
  • Death Domain Receptor Signaling Adaptor Proteins
  • FADD protein, human
  • Fas-Associated Death Domain Protein
  • RNA, Double-Stranded
  • Receptors, Tumor Necrosis Factor
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
  • CASP8 protein, human
  • Caspase 8
  • Caspases