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Death Effector Domain-Containing Proteins
- Source :
- Cellular and Molecular Life Sciences. 66:814-830
- Publication Year :
- 2008
- Publisher :
- Springer Science and Business Media LLC, 2008.
-
Abstract
- 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 (TNFalpha) 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.
- Subjects :
- Models, Molecular
Death Domain Receptor Signaling Adaptor Proteins
Programmed cell death
GTPase-activating protein
Protein Conformation
DEDD
Apoptosis
Biology
Cellular and Molecular Neuroscience
Morphogenesis
Animals
Humans
Protein Isoforms
FADD
Molecular Biology
Cell Proliferation
Death domain
Pharmacology
Effector
Cell Biology
Cell biology
biology.protein
Molecular Medicine
Death effector domain
Signal transduction
Signal Transduction
Subjects
Details
- ISSN :
- 14209071 and 1420682X
- Volume :
- 66
- Database :
- OpenAIRE
- Journal :
- Cellular and Molecular Life Sciences
- Accession number :
- edsair.doi.dedup.....d4e780f0af8f4e2370d1c23c042adbdd
- Full Text :
- https://doi.org/10.1007/s00018-008-8489-0