BAIT

FADD

Mort1/FADD
Fas (TNFRSF6)-associated via death domain
GO Process (34)
GO Function (8)
GO Component (9)

Gene Ontology Biological Process

Mus musculus
PREY

ATG16L1

1500009K01Rik, Apg16l, Atg16l, WDR30
autophagy related 16-like 1 (S. cerevisiae)
GO Process (2)
GO Function (2)
GO Component (3)
Mus musculus

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells.

Bell BD, Leverrier S, Weist BM, Newton RH, Arechiga AF, Luhrs KA, Morrissette NS, Walsh CM

Fas-associated death domain protein (FADD) and caspase-8 (casp8) are vital intermediaries in apoptotic signaling induced by tumor necrosis factor family ligands. Paradoxically, lymphocytes lacking FADD or casp8 fail to undergo normal clonal expansion following antigen receptor cross-linking and succumb to caspase-independent cell death upon activation. Here we show that T cells lacking FADD or casp8 activity are subject to hyperactive ... [more]

Proc. Natl. Acad. Sci. U.S.A. Oct. 28, 2008; 105(43);16677-82 [Pubmed: 18946037]

Throughput

  • Low Throughput

Curated By

  • BioGRID