Proximity Ligation Analysis of protein-protein interactions between FADD and FAS. HeLa cells were stained with anti-FADD rabbit purified polyclonal 1:1200 and anti-FAS mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex, and nuclei were counterstained with DAPI (blue).
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The interaction of this receptor with its ligand allows the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10. The autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, and leads to apoptosis. This receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is found to be involved in transducing the proliferating signals in normal diploid fibroblast and T cells. At least eight alternatively spliced transcript variants have been described, some of which are candidates for nonsense-mediated decay (NMD). The isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform. [provided by RefSeq
APO-1 cell surface antigen,CD95 antigen,Fas AMA,Fas antigen,OTTHUMP00000020045,OTTHUMP00000020046,OTTHUMP00000020051,OTTHUMP00000059646,apoptosis antigen 1,tumor necrosis factor receptor superfamily member 6,tumor necrosis factor receptor superfamily, mem