Description
Product Characteristics:
FADD (Fas Associated Death Domain) is an apoptosis adapter molecule enabling transduction of the apoptosis signal initiated via the FasL/Fas receptor interaction. The protein contains a C terminal death domain that interacts with the Fas receptor death domain. The N terminus contains a death effectors domain (DED) which recruits caspase to the death inducing signaling complex (DISC) and initiates the apoptotic caspase cascade. Recruitment of Caspase 8 to the Fas receptor results in oligomerization of the Caspase 8 protein, which in turn drives its autoactivation through self-cleavage. Activated Caspase 8 then activates other downstream caspases including Caspase 9, thereby commiting the cell to undergo apoptosis. FADD is implicated in non-apoptotic cellular pathways such as the regulation of cell cycle machinery in T lymphocytes. This is connected to the phosphorylation state of FADD and to the FasL/TRAIL induced transcriptional activation of cfos protooncogene. FADD also interacts with the hepatitis C virus core protein in the HEK 293 cell line.
Synonyms: FADD phospho S194, p-FADD phospho S194, P-Fas-associated protein with death domain, FADD protein, Fas TNFRSF6 associated via death domain, Fas associated via death domain, Fas associating death domain containing protein, Fas associating protein, Fas associating protein with death domain, Fas TNFRSF6 associated via death domain, GIG 3, GIG3, Growth inhibiting gene 3 protein, H sapiens mRNA for mediator of receptor induced toxicity, Mediator of receptor induced toxicity, MGC8528, MORT 1, MORT1.
Target Information: The protein encoded by this gene is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and thus it participates in the death signaling initiated by these receptors. Interaction of this protein with the receptors unmasks the N-terminal effector domain of this protein, which allows it to recruit caspase-8, and thereby activate the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development. [provided by RefSeq, Jul 2008]