DED or alive: assembly and regulation of the death effector domain complexes

Cell Death Dis. 2015 Aug 27;6(8):e1866. doi: 10.1038/cddis.2015.213.

Abstract

Death effector domains (DEDs) are protein-protein interaction domains initially identified in proteins such as FADD, FLIP and caspase-8 involved in regulating apoptosis. Subsequently, these proteins have been shown to have important roles in regulating other forms of cell death, including necroptosis, and in regulating other important cellular processes, including autophagy and inflammation. Moreover, these proteins also have prominent roles in innate and adaptive immunity and during embryonic development. In this article, we review the various roles of DED-containing proteins and discuss recent developments in our understanding of DED complex formation and regulation. We also briefly discuss opportunities to therapeutically target DED complex formation in diseases such as cancer.

Publication types

  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry*
  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Antineoplastic Agents / chemical synthesis
  • Antineoplastic Agents / therapeutic use
  • Apoptosis / drug effects
  • Autophagy / drug effects
  • Caspase 8 / chemistry*
  • Caspase 8 / genetics
  • Caspase 8 / metabolism
  • Clinical Trials as Topic
  • Fas-Associated Death Domain Protein / chemistry*
  • Fas-Associated Death Domain Protein / genetics
  • Fas-Associated Death Domain Protein / metabolism
  • Gene Expression Regulation, Neoplastic*
  • Humans
  • Mice
  • Models, Molecular
  • Neoplasms / drug therapy
  • Neoplasms / genetics*
  • Neoplasms / metabolism
  • Neoplasms / pathology
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Signal Transduction

Substances

  • Adaptor Proteins, Signal Transducing
  • Antineoplastic Agents
  • FADD protein, human
  • Fas-Associated Death Domain Protein
  • TNIP2 protein, human
  • Caspase 8