cd08336

Death Effector Domain found in Fas-Associated via Death Domain

CDD entry
Member databaseCDD
CDD typedomain
Short nameDED_FADD
SetDD

Description

Death Effector Domain (DED) found in Fas-Associated via Death Domain (FADD). DEDs comprise a subfamily of the Death Domain (DD) superfamily. FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor and its DED recruits the initiator caspases 8 and 10 to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.
[15, 5, 4, 12, 6, 1, 16, 9, 10, 8, 7, 2, 14, 3, 11, 13]

References

1.The FADD is going nuclear. Sheikh MS, Huang Y. Cell Cycle 2, 346-7, (2003). PMID: 12851487

2.The death effector domain protein family: regulators of cellular homeostasis. Tibbetts MD, Zheng L, Lenardo MJ. Nat. Immunol. 4, 404-9, (2003). View articlePMID: 12719729

3.The structure of FADD and its mode of interaction with procaspase-8. Carrington PE, Sandu C, Wei Y, Hill JM, Morisawa G, Huang T, Gavathiotis E, Wei Y, Werner MH. Mol. Cell 22, 599-610, (2006). View articlePMID: 16762833

4.Nuclear localized phosphorylated FADD induces cell proliferation and is associated with aggressive lung cancer. Bhojani MS, Chen G, Ross BD, Beer DG, Rehemtulla A. Cell Cycle 4, 1478-81, (2005). PMID: 16258269

5.Molecular roles of MAP kinases and FADD phosphorylation in prostate cancer. Shimada K, Nakamura M, Ishida E, Konishi N. Histol Histopathol 21, 415-22, (2006). PMID: 16437387

6.FADD and its phosphorylation. Zhang J, Zhang D, Hua Z. IUBMB Life 56, 395-401, (2004). PMID: 15545216

7.FLIP and the death effector domain family. Yu JW, Shi Y. Oncogene 27, 6216-27, (2008). PMID: 18931689

8.Death effector domain-containing proteins. Valmiki MG, Ramos JW. Cell Mol Life Sci 66, 814-30, (2009). PMID: 18989622

9.The death domain superfamily: a tale of two interfaces? Weber CH, Vincenz C. Trends Biochem. Sci. 26, 475-81, (2001). View articlePMID: 11504623

10.Playing the DISC: turning on TRAIL death receptor-mediated apoptosis in cancer. Pennarun B, Meijer A, de Vries EG, Kleibeuker JH, Kruyt F, de Jong S. Biochim Biophys Acta 1805, 123-40, (2010). PMID: 19961901

11.NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. Eberstadt M, Huang B, Chen Z, Meadows RP, Ng SC, Zheng L, Lenardo MJ, Fesik SW. Nature 392, 941-5, (1998). View articlePMID: 9582077

12.Multifunctional role of Fas-associated death domain protein in apoptosis. Kim KS. J Biochem Mol Biol 35, 1-6, (2002). PMID: 16248963

13.Rewinding the DISC. Chaigne-Delalande B, Moreau JF, Legembre P. Arch Immunol Ther Exp (Warsz) 56, 9-14, (2008). PMID: 18250974

14.The death domain superfamily in intracellular signaling of apoptosis and inflammation. Park HH, Lo YC, Lin SC, Wang L, Yang JK, Wu H. Annu. Rev. Immunol. 25, 561-86, (2007). View articlePMID: 17201679

15.Emerging roles for the death adaptor FADD in death receptor avidity and cell cycle regulation. Werner MH, Wu C, Walsh CM. Cell Cycle 5, 2332-8, (2006). PMID: 17102623

16.FADD/MORT1, a signal transducer that can promote cell death or cell growth. Strasser A, Newton K. Int J Biochem Cell Biol 31, 533-7, (1999). PMID: 10399313

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