FADD
FADD (Fas associated via death domain, also known as MORT1 and GIG3) is a cytoplasmic adaptor protein that links death receptors to the caspase machinery. It recruits caspase-8 or caspase-10 to activated receptors, initiating the apoptotic cascade. Browse Assay Genie's current range of FADD research reagents below, or read on for the biology behind the target.
FADD is an apoptotic adapter molecule that recruits caspase-8 (CASP8) or caspase-10 (CASP10) to activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors. The resulting aggregate, the death-inducing signalling complex (DISC), performs proteolytic activation of caspase-8, and active caspase-8 then initiates the downstream cascade of caspases that mediates apoptosis. FADD is also involved in the interferon-mediated antiviral immune response, where it positively regulates interferon signalling.
The FADD protein works through two domains. Its C-terminal death domain allows it to be recruited by receptors including TNFRSF6/Fas receptor, tumour necrosis factor receptor, TNFRSF25 and the TNFSF10/TRAIL receptors, so that it participates in the death signalling these receptors initiate. Receptor interaction unmasks the N-terminal effector domain, which recruits caspase-8 and activates the cysteine protease cascade. The FADD gene is annotated in the HGNC groups for death effector domain-containing proteins, the ripoptosome and the death inducing signalling complex, and the protein localises to the cytoplasm.
The gene symbol FADD derives from the previous name Fas (TNFRSF6)-associated via death domain; MORT1 and GIG3 are alternative names. Knockout studies in mice, which carry the orthologous Fadd gene, also suggest that FADD is important in early T cell development. This combination of roles makes FADD a common focus for studies of cell death and immune signalling.
FADD couples death receptors to caspase-8 and caspase-10, making it central to studies of extrinsic apoptosis.
FADD is recruited by Fas, TNFR1, TNFRSF25 and TRAIL receptors, allowing comparison of signalling across these receptors.
FADD plays a role in the positive regulation of interferon signalling during the interferon-mediated antiviral immune response.
Knockout studies in mice indicate that FADD is important for early T cell development.
FADD is an adaptor protein that is recruited to activated death receptors such as FAS/CD95 and TNFR-1 through its death domain. It then recruits caspase-8 or caspase-10, forming the DISC, which activates caspase-8 and starts the apoptotic caspase cascade. It also supports interferon signalling.
FADD stands for Fas associated via death domain and is also known as MORT1 and GIG3. HGNC lists the previous name Fas (TNFRSF6)-associated via death domain. UniProt names the protein FAS-associated death domain protein. These names all refer to the same gene and protein.
A mouse ortholog, Fadd, exists, and knockout studies in mice suggest FADD is important in early T cell development. Check the datasheet of any product for its validated reactivity before use in a given species.
Other death receptors, caspases and apoptosis pathway proteins that work alongside FADD.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13158; product specifications from Assay Genie datasheets.