The BioGRID | PUBLICATION VIEW

	Nat. Immunol. Jun (2001); 2(6):493-500
A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins.
Miyazaki T, Reed JC
The Burnham Institute, 10901 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Abstract: Apoptosis-inducing tumor necrosis factor (TNF) family receptors recruit the proforms of caspase family cell death proteases to ligand-receptor complexes through interactions with intracellular adapter proteins. We have found that the GTP-binding protein DAP3 binds directly (with high affinity) to the death domain of TNF-related apoptosis-inducing ligand (TRAIL) receptors, and is required for TRAIL-induced apoptosis. DAP3 also associates with the pro-caspase-8--binding adapter protein Fas-associated death domain (FADD), and links FADD to the TRAIL receptors DR4 and DR5. We have also found that binding of DAP3 to FADD and activation of pro-caspase-8 in an in vitro reconstituted system is GTP-dependent. Elucidation of this mechanism suggests GTP-binding proteins as potential targets for pharmacological intervention in TRAIL-induced apoptosis.
[PUBMED: 11376335]