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The present data suggests FADD as a putative biomarker for pathological processes associated with the course of clinical dementia.
at normal levels of expression during bacterial infection, NleB1/NleB(CR) antagonizes death receptor-induced apoptosis of infected cells by modifying FADD in an irreversible manner.
Caspase-8 can serve in two distinct roles in response to TRAIL receptor engagement, as a scaffold for assembly of a Caspase-8-FADD-RIPK1 "FADDosome" complex, leading to NFkappaB-dependent inflammation, or as a protease that promotes apoptosis.
Using the tDED filament structure as a template, structural analyses reveal the interaction surfaces between FADD and caspase-8 (show CASP8 Proteins) and the distinct mechanisms of regulation by cFLIP (show CFLAR Proteins) and MC159 through comingling and capping, respectively.
This study reveals an essential role of SUMOylated FADD in Drp1 (show CRMP1 Proteins)- and caspase-10 (show CASP10 Proteins)-dependent necrosis.
In myelodysplastic syndrome, FADD expression is regulated by SPAG6 (show SPAG6 Proteins) which influences its interaction with TRAIL death receptors.
High levels of FADD and caspase-8 (show CASP8 Proteins), but not caspase-3 (show CASP3 Proteins), were associated with increased incidence of coronary events in subjects from the general population.
Both Fas associated via death domain gene copy number amplification and high protein expression were significantly associated with lymph node metastasis and had the shortest disease-free survival and overall survival.
FADD, as well as NEMO, is a substrate for LUBAC ubiquitin ligase (E3) complex, composed of the HOIP, HOIL-1L, and SHARPIN subunits.
autoinflammation-associated H443P nlrc4 (show NLRC4 Proteins) mutant is altered in interaction with SUG1 (show PSMC5 Proteins) and ubiquitinated proteins, triggering constitutive caspase-8 (show CASP8 Proteins)-mediated cell death dependent on FADD but independent of Ser (show SIGLEC1 Proteins)(533) phosphorylation.
The authors conclude that FADD is a master regulator of glucose and fat metabolism.
Mice deficient in RIPK3 (show RIPK3 Proteins) or doubly deficient in MLKL and FADD, but not MLKL alone, are more susceptible to influenza A virus than their wild-type counterparts, revealing an important role for RIPK3 (show RIPK3 Proteins)-mediated apoptosis in antiviral immunity.
Wild-type cells can execute apoptosis via both, the mitochondrial and the receptor-mediated pathway whereas FADD-deficient cells can only activate the intrinsic pathway. There is a difference in UVC radiation response between two cell lines indicating the role of FADD in the selection of cell death modality.
knockdown of cFLIPL and induced expression of FADD rapidly accumulate intracellular ROS (show ROS1 Proteins) accompanied by JNK1 (show MAPK8 Proteins) activation to substantiate apoptosis.
A20 targets caspase-8 and FADD to protect HTLV-I-infected cells.
Deletion of FADD in macrophages and granulocytes results in RIP3- and MyD88 (show MYD88 Proteins)-dependent systemic inflammation.
A constitutively phosphoryl-mimicking mutation of Fas (show FAS Proteins)-associated death domain (FADD-D) enhances Notch-1 (show NOTCH1 Proteins) signaling and compromises Wnt (show WNT2 Proteins) signaling in both cultured myoblasts and regenerating muscles.
Beta amyloid-induced upregulation of death receptor 6 (show TNFRSF21 Proteins) accelerates the toxic effect of N-terminal fragment of amyloid precursor protein (show APP Proteins)
Phosphorylation of FADD by the kinase CK1alpha (show CSNK1A1 Proteins) promotes KRASG12D-induced lung cancer.
FADD induces apoptosis
mapping and sequencing of bovine FADD cDNA, and characterization of its expression in endothelial cells
FADD has multiple functions in embryos; it plays a part in the regulation of NF-kappaB (show NFKB1 Proteins) activation and heart formation, in addition to apoptosis.
The FADD protein shows evolutionary conservation.
Interaction of xFADD and xRIP1 induced synergistic activation of JNK (show MAPK8 Proteins) and NF-kappaB (show NFKB1 Proteins).
establish that pax2 in combination with vax2 directly regulate the fas-associated death domain (fadd) gene
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.
Fas-associating death domain-containing protein
, Fas-associating protein with death domain
, growth-inhibiting gene 3 protein
, mediator of receptor induced toxicity
, mediator of receptor-induced toxicity
, protein FADD
, FAS-associated death domain protein
, FAS-associating death domain-containing protein
, Fas (TNF receptor superfamily, member 6)
, Fas-associated via death domain
, Fas (TNFRSF6)-associated via death domain
, Fas associated via death domain S homeolog