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| Content Provider | Springer Nature Link |
|---|---|
| Author | Valmiki, M. Gudur Ramos, J. W. |
| Copyright Year | 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 α (TNFα) 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. |
| Starting Page | 814 |
| Ending Page | 830 |
| Page Count | 17 |
| File Format | |
| ISSN | 1420682X |
| Journal | Cellular and Molecular Life Sciences |
| Volume Number | 66 |
| Issue Number | 5 |
| e-ISSN | 14209071 |
| Language | English |
| Publisher | Birkhäuser-Verlag |
| Publisher Date | 2008-11-08 |
| Publisher Place | Basel |
| Access Restriction | Subscribed |
| Subject Keyword | Death effector domain apoptosis proliferation signal transduction migration caspase FADD Cell Biology Biomedicine general Life Sciences Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience |
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