FAS-associated death domain protein

Definition:

Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling.

References:

[1]. Alexandre Bolze, et al. Whole-exome-sequencing-based discovery of human FADD deficiency. Am J Hum Genet. 2010 Dec 10;87(6):873-81. [Content Brief]

[2]. Paul E Carrington, et al. The structure of FADD and its mode of interaction with procaspase-8. Mol Cell. 2006 Jun 9;22(5):599-610. [Content Brief]

[3]. Shan Li, et al. Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains. Nature. 2013 Sep 12;501(7466):242-6. [Content Brief]

[4]. Fiona L Scott, et al. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature. 2009 Feb 19;457(7232):1019-22. [Content Brief]

[5]. Jaclyn S Pearson, et al. A type III effector antagonizes death receptor signalling during bacterial gut infection. Nature. 2013 Sep 12;501(7466):247-51. [Content Brief]

[6]. A M Chinnaiyan, et al. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell. 1995 May 19;81(4):505-12. [Content Brief]

[7]. Liwei Wang, et al. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat Struct Mol Biol. 2010 Nov;17(11):1324-9. [Content Brief]

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