BAIT

CASP8

ALPS2B, CAP4, Casp-8, FLICE, MACH, MCH5
caspase 8, apoptosis-related cysteine peptidase
GO Process (33)
GO Function (9)
GO Component (10)

Gene Ontology Biological Process

Homo sapiens
PREY

MAPK1

ERK, ERK-2, ERK2, ERT1, MAPK2, P42MAPK, PRKM1, PRKM2, p38, p40, p41, p41mapk, p42-MAPK
mitogen-activated protein kinase 1
GO Process (46)
GO Function (4)
GO Component (14)

Gene Ontology Biological Process

Homo sapiens

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

Death effector domain DEDa, a self-cleaved product of caspase-8/Mch5, translocates to the nucleus by binding to ERK1/2 and upregulates procaspase-8 expression via a p53-dependent mechanism.

Yao Z, Duan S, Hou D, Heese K, Wu M

Activation of the apical caspase-8 is crucial to the extrinsic apoptotic pathway. Although the death effector domain (DED) of caspase-8 has been reported to be involved in death-inducing signaling complex formation, the detailed mechanism of how DED functions in regulating apoptosis remains largely unknown. Here, we demonstrate that the prodomain of the caspase-8/Mch5 can be further cleaved between two tandemly ... [more]

EMBO J. Feb. 21, 2007; 26(4);1068-80 [Pubmed: 17290218]

Throughput

  • Low Throughput

Curated By

  • BioGRID