4.7 Review

Death Effector Domain-Containing Proteins

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 66, Issue 5, Pages 814-830

Publisher

SPRINGER BASEL AG
DOI: 10.1007/s00018-008-8489-0

Keywords

Death effector domain; apoptosis; proliferation; signal transduction; migration; caspase; FADD

Funding

  1. National Institutes of Health [NCI CA93849]
  2. Department of Defense [05245002]
  3. Hawaii Community Foundation [20061496]
  4. NATIONAL CANCER INSTITUTE [R56CA093849, R01CA093849] Funding Source: NIH RePORTER

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Death effector domains (DEDs) are protein-protein interaction structures that are found in proteins that regulate a variety of signal transduction pathways. DEDs are a part of the larger family of Death Domain structures that have been primarily described in the control of programmed cell death. The seven standard DED-containing proteins are fas associated death domain protein (FADD), Caspase-8 and 10, cellular FLICE-like inhibitory protein (c-FLIP), death effector domain containing DNA binding (DEDD), DEDD2 and phosphoprotein enriched in astrocytes 15-Kda (PEA-15). These proteins are particularly associated with the regulation of apoptosis and proliferation mediated by the tumor necrosis factor alpha (TNF alpha) receptor family. Consequently DED-containing proteins are reported to regulate transcription, migration, and proliferation, in addition to both pro and anti-apoptotic functions. Moreover, DED proteins are essential in embryonic development and homeostasis of the immune system. Here we focus on the role of DED-containing proteins in development and the pathologies arising from abnormal expression of these proteins.

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