RAIDD is a new 'death' adaptor molecule

  title={RAIDD is a new 'death' adaptor molecule},
  author={Hangjun Duan and Vishva M. Dixit},
THE effector arm of the cell-death pathway is composed of cysteine proteases belonging to the ICE/CED-3 family1,2. In metazoan cells these exist as inactive polypeptide precursors (zymogens), each composed of a prodomain, which is cleaved to activate the protease, and a large and small catalytic subunit. The coupling of these 'death' proteases to signalling pathways is probably mediated by adaptor molecules that contain protein–protein interaction motifs such as the death domain1. Here we… 

dFADD, a Novel Death Domain-containing Adapter Protein for theDrosophila Caspase DREDD*

Apoptotic cell death occurs through activation of procaspases, the precursors of a group of aspartate-specific cysteine proteases known as caspases. Procaspase activation is mediated by death adapter

Caspases: the executioners of apoptosis.

  • G. Cohen
  • Biology
    The Biochemical journal
  • 1997
The importance of caspase prodomains in the regulation of apoptosis is further highlighted by the recognition of adapter molecules, such as RAIDD [receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of cspase-2 and recruits it to the signalling complex.

Death domain receptors and their role in cell demise.

  • A. SinghJ. NiB. Aggarwal
  • Biology
    Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research
  • 1998
Because numerous proteins that mediate apoptosis have been discovered independently and simultaneously and thus are known by many different names, a comprehensive cross-referenced list of these proteins is provided.

NMR structure and mutagenesis of the FADD (Mort1) death-effector domain

A hydrophobic region of the FADD death-effector domain that is not present in the death domains is vital for binding to FLICE and for apoptotic activity.

CASH, a Novel Caspase Homologue with Death Effector Domains*

The findings suggest that CASH acts as an attenuator and/or initiator in CD95 and CD120a signaling for cell death, through a shared N-terminal sequence motif, the death effector domain.

Death receptors and their ligands

The identification and description of an intrinsic program of regulated cellular suicide or apoptosis was originally obtained from morphological analyses in developmental biology and genetic analyses in the nematode Caenorhabditis elegans.

The Death Domain Superfamily in Intracellular Signaling of Apoptosis and Inflammation

This chapter reviews the molecular complexes assembled by these proteins, the structural and biochemical features of these domains, and the molecular interactions mediated by them to provide a comprehensive understanding of the function, structure, interaction, and evolution of this important family of domains.

Identification of CARDIAK, a RIP-like kinase that associates with caspase-1

Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD

It is demonstrated that endogenous RAIDD is mostly localized in the cytoplasm and to some extent in the nucleus, and evidence that RAIDD-CARD oligomerization may be regulated by intramolecular folding of the RAIDD molecule is presented.



Fas- and Tumor Necrosis Factor-induced Apoptosis Is Inhibited by the Poxvirus crmA Gene Product (*)

CrmA was found to be an exceptionally potent inhibitor of apoptosis induced by both Fas- and tumor necrosis factor-induced cell death pathways, capable of blocking the cell death program even at pharmacological doses of the death stimulus.

Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities.

The results suggest a genetic pathway for programmed cell death in Caenorhabditis elegans in which ced-4 acts upstream of or in parallel to cing-3 and ces-9 negatively regulates the activity of ceden-4.