Cellular and Molecular Life Sciences

, Volume 66, Issue 5, pp 814–830

Death Effector Domain-Containing Proteins

Authors

  • M. Gudur Valmiki
    • Department of Molecular Biosciences and BioengineeringUniversity of Hawaii at Manoa
    • Department of Natural Products and Cancer Biology, Cancer Research Center of HawaiiUniversity of Hawaii at Manoa
    • Department of Natural Products and Cancer Biology, Cancer Research Center of HawaiiUniversity of Hawaii at Manoa
Review

DOI: 10.1007/s00018-008-8489-0

Cite this article as:
Valmiki, M.G. & Ramos, J.W. Cell. Mol. Life Sci. (2009) 66: 814. doi:10.1007/s00018-008-8489-0

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.

Keywords.

Death effector domain apoptosis proliferation signal transduction migration caspase FADD

Copyright information

© Birkhäuser Verlag, Basel 2008