FADD

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FADD death effector domain

PDB rendering based on 1a1w.

Available structures: 1a1w, 1a1z, 1e3y, 1e41, 2gf5

Identifiers

Symbol(s)

FADD; GIG3; MGC8528; MORT1

External IDs

OMIM: 602457 MGI: 109324 HomoloGene: 2836

Gene ontology
Molecular Function:	• signal transducer activity • death receptor binding • protein kinase binding • identical protein binding
Cellular Component:	• cytoplasm
Biological Process:	• cell surface receptor linked signal transduction • induction of apoptosis via death domain receptors • apoptotic program • antimicrobial humoral response • regulation of apoptosis • positive regulation of I-kappaB kinase/NF-kappaB cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003824 (mRNA)
NP_003815 (protein)

NM_010175 (mRNA)
NP_034305 (protein)

Location

Chr 11: 69.73 - 69.73 Mb

Chr 7: 144.39 - 144.39 Mb

Pubmed search

[1]

[2]

Fas-Associated protein with Death Domain (FADD) is an adaptor molecule that bridges the Fas-receptor, and other death receptors, to caspase-8 through its death domain to form the death inducing signaling complex (DISC) during apoptosis. 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^[1](see structural image on the right side) 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.^[2]

Signaling pathway of TNF-R1. Dashed grey lines represent multiple steps

1 References
2 Further reading
3 See also
4 External links

[edit] References

^ Eberstadt M, et al. (1998). "NMR structure and mutagenesis of the FADD (Mort1) death-effector domain". Nature 391: 941–5. doi:10.1038/31972.
^ Entrez Gene: FADD Fas (TNFRSF6)-associated via death domain.

[edit] Further reading

Sheikh MS, Huang Y (2004). "The FADD is going nuclear.". Cell Cycle 2 (4): 346–7. PMID 12851487.
Bhojani MS, Chen G, Ross BD, et al. (2007). "Nuclear localized phosphorylated FADD induces cell proliferation and is associated with aggressive lung cancer.". Cell Cycle 4 (11): 1478–81. PMID 16258269.