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FADD

GeneName

FADD

Summary

FADD, also known as Fas associated death domain protein, is a 23kDa adaptor protein that plays a pivotal role in the apoptotic process. It is primarily localised in the cytoplasm and plasma membrane, where it participates in the formation of death-inducing signalling complexes (DISCs) and ripoptosomes. FADD interacts with death receptors, such as CD95, and is essential for transducing apoptotic signals through caspase activation. Additionally, it is involved in various immune responses, including the regulation of T cell activation and differentiation, as well as responses to viral infections.

Importance

FADD is relevant to: - Apoptosis and its regulation, which is crucial for maintaining cellular homeostasis and eliminating damaged cells - Immune responses, particularly in T cell activation and differentiation, impacting adaptive immunity - Cancer research, as dysregulation of apoptotic pathways involving FADD can contribute to tumourigenesis - Neurodegenerative diseases, where apoptosis plays a role in neuronal loss - Viral pathogenesis, as FADD mediates host defence mechanisms against viral infections

Top Products

For researchers investigating FADD, we highly recommend the top-selling recombinant antibody, Anti-FADD antibody [EPR4415] (ab108601). This well-cited antibody has garnered 16 citations, reflecting its reliability and trust within the research community. It has been validated in knockout models and is suitable for a variety of applications, including Western blotting (WB), immunoprecipitation (IP), immunohistochemistry (IHC), and flow cytometry (FC). This versatility makes it an excellent choice for those requiring consistent and effective detection of FADD in their studies.

Abcam Product Citation Summary

The data indicates that FADD is being investigated in the context of cell migration and necroptosis, with studies conducted on various cell types including melanoma cells and human umbilical vein endothelial cells. The use of western blotting suggests a focus on protein expression levels in these biological processes.

Abcam Product Citation Table

Product Code
Species
Application
Study Context
PMID
ab108601
Mouse
WB
Cell migration
27286445
ab108601
Human
WB
Cell migration
27286445
ab108601
Human
WB
Necroptosis
33597510

Domain

Contains a death domain involved in the binding of the corresponding domain within Fas receptor.

The interaction between the FAS and FADD death domains is crucial for the formation of the death-inducing signaling complex (DISC).

Function

Apoptotic adapter molecule that recruits caspases CASP8 or CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:23955153, PubMed:24025841, PubMed:7538907, PubMed:9184224). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:7538907, PubMed:9184224). Active CASP8 initiates the subsequent cascade of caspases mediating apoptosis (PubMed:16762833). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (PubMed:21109225).

Involvement in disease

Infections, recurrent, associated with encephalopathy, hepatic dysfunction and cardiovascular malformations

IEHDCM

A condition with biological features of autoimmune lymphoproliferative syndrome such as high-circulating CD4(-)CD8(-)TCR-alpha-beta(+) T-cell counts, and elevated IL10 and FASL levels. Affected individuals suffer from recurrent, stereotypical episodes of fever, encephalopathy, and mild liver dysfunction sometimes accompanied by generalized seizures. The episodes can be triggered by varicella zoster virus (VZV), measles mumps rubella (MMR) attenuated vaccine, parainfluenza virus, and Epstein-Barr virus (EBV).

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

(Microbial infection) Glycosylated at Arg-117 by enteropathogenic E.coli protein NleB1, C.rodentium protein NleB and S.typhimurium protein Ssek1: arginine GlcNAcylation prevents recruitment of caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors.

Tissue Specificity

Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes.

Alternative names

MORT1, GIG3, FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Growth-inhibiting gene 3 protein, Mediator of receptor induced toxicity

swissprot:Q13158 entrezGene:8772 omim:602457