Review:Death Domain Receptors and Their Role in Cell Demise
- 1 July 1998
- journal article
- review article
- Published by Mary Ann Liebert Inc in Journal of Interferon & Cytokine Research
- Vol. 18 (7) , 439-450
- https://doi.org/10.1089/jir.1998.18.439
Abstract
Apoptotic signals are transduced by five death domain-containing receptors—TNFR1, Fas, DR3, DR4, and DR5—by binding to their iigands. The intracellular portion of all these receptors contains a region, approximately 80 amino acids long, referred to as the "death domain" (DD). On activation by its ligand, the DD recruits various proteins that mediate cell death. These proteins, in turn, recruit other proteins via their DDs or death effector domains (DED). The actual destruction of the cell, however, is accomplished by serial activation of a family of proteases referred to as caspases. Cell death is, in part, regulated by transmembrane decoy receptors that contain either none of or only part of the DD. This article briefly reviews what is known about the receptors and other proteins involved in apoptosis. In addition, because numerous proteins that mediate apoptosis have been discovered independently and simultaneously and thus are known by many different names, a comprehensive cross-referenced list of these proteins is provided.Keywords
This publication has 126 references indexed in Scilit:
- ERICE, a Novel FLICE-activatable CaspasePublished by Elsevier ,1998
- Apo-3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-κBCurrent Biology, 1996
- Increased Expression of the Insulin-like Growth Factor-II Gene in Wilms' Tumor Is Not Dependent on Loss of Genomic Imprinting or Loss of HeterozygosityPublished by Elsevier ,1996
- Involvement of MACH, a Novel MORT1/FADD-Interacting Protease, in Fas/APO-1- and TNF Receptor–Induced Cell DeathCell, 1996
- Induction of Apoptosis by Apo-2 Ligand, a New Member of the Tumor Necrosis Factor Cytokine FamilyJournal of Biological Chemistry, 1996
- TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling ComplexImmunity, 1996
- A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40FEBS Letters, 1995
- A Lymphotoxin-β-Specific ReceptorScience, 1994
- A novel domain within the 55 kd TNF receptor signals cell deathCell, 1993
- Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxinNature, 1984