Home  |  Contact
PROSITE documentation PDOC50168 [for PROSITE entry PS50168]

Death effector domain (DED) profile





Description

The apoptotic signal coming from ligand-induced oligomerization of death receptors is mediated by a number of adaptor proteins containing specialized interaction domains. Besides the death effector domain (DED), this group is formed by the death domain (DD) (see <PDOC50017>) and the caspase recruitment domain (CARD) (see <PDOC50209>).

The death effector domain was first described in the FADD/Mort1 protein [1] and later shown to also occur in several other proteins [2,3]. The DED typically associates with other DED-containing proteins, forming either dimers or trimers [2,3,4]. It has been predicted that the DED is related in structure and sequence to both DD and CARD domains, which work in similar pathways and show similar interaction properties [5]. Important members of the DED family are:

  • FADD/MORT1 death adaptor protein.
  • Caspase-8 (EC 3.4.22.-), upstream death protease, interacts with FADD.
  • Caspase-10 (EC 3.4.22.-).
  • v-FLIP, FLICE(caspase)-inhibitors that occur in γ herpesviruses and the poxvirus MCV, interact with FADD and/or Caspase-8.
  • c-FLIP, cellular FLICE-inhibitor with inactive caspase domain, interacts with FADD and/or caspase-8.
  • PEA15, a brain-specific phosphoprotein of unknown function
Note:

The profile covers the complete domain.

Expert(s) to contact by email:

Hofmann K.

Last update:

December 2001 / First entry.

-------------------------------------------------------------------------------

Technical section

PROSITE method (with tools and information) covered by this documentation:

DED, PS50168; Death effector domain (DED) profile  (MATRIX)


References

1AuthorsChinnaiyan A.M. O'Rourke K. Tewari M. Dixit V.M.
TitleFADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.
SourceCell 81:505-512(1995).
PubMed ID7538907

2AuthorsThome M. Schneider P. Hofmann K. Fickenscher H. Meinl E. Neipel F. Mattmann C. Burns K. Bodmer J.L. Schroter M. Scaffidi C. Krammer P.H. Peter M.E. Tschopp J.
TitleViral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors.
SourceNature 386:517-521(1997).
PubMed ID9087414

3AuthorsIrmler M. Thome M. Hahne M. Schneider P. Hofmann K. Steiner V. Bodmer J.L. Schroter M. Burns K. Mattmann C. Rimoldi D. French L.E. Tschopp J.
TitleInhibition of death receptor signals by cellular FLIP.
SourceNature 388:190-195(1997).
PubMed ID9217161
DOI10.1038/40657

4AuthorsMuzio M. Chinnaiyan A.M. Kischkel F.C. O'Rourke K. Shevchenko A. Ni J. Scaffidi C. Bretz J.D. Zhang M. Gentz R. Mann M. Krammer P.H. Peter M.E. Dixit V.M.
TitleFLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex.
SourceCell 85:817-827(1996).
PubMed ID8681377

5AuthorsHofmann K. Bucher P. Tschopp J.
TitleThe CARD domain: a new apoptotic signalling motif.
SourceTrends Biochem. Sci. 22:155-156(1997).
PubMed ID9175472



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)