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CARD8 — CASP1
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind_translation Interaction:
CARD8
—
CASP1
(affinity chromatography technology)
Razmara et al., J Biol Chem 2002*
-
IRef Bind_translation Interaction:
CARD8
—
CASP1
(coimmunoprecipitation)
Razmara et al., J Biol Chem 2002*
-
IRef Hprd Interaction:
CASP1
—
CARD8
(in vivo)
Razmara et al., J Biol Chem 2002*
-
IRef Hprd Interaction:
CASP1
—
CARD8
(in vitro)
Razmara et al., J Biol Chem 2002*
-
IRef Innatedb Interaction:
CARD8
—
CASP1
(unknown, -)
Wagner et al., PloS one 2009*
-
IRef Innatedb Interaction:
CARD8
—
CASP1
(unknown, -)
Razmara et al., J Biol Chem 2002*
-
IRef Innatedb Interaction:
CARD8
—
CASP1
(unknown, -)
Agostini et al., Immunity 2004
-
IRef Innatedb Interaction:
Complex of CASP1-CARD8-PYCARD-NLRP3-NLRP3-CASP1-CARD8-PYCARD
(unknown, -)
Agostini et al., Immunity 2004
-
IRef Innatedb Interaction:
Complex of NLRP2-CARD8-CARD8-PYCARD-PYCARD-CASP1-NLRP2-CASP1
(unknown, -)
Agostini et al., Immunity 2004
Text-mined interactions from Literome
Zhou et al., Proc Natl Acad Sci U S A 1999
:
Direct recruitment and
activation of
caspase-9 by Apaf-1 through the homophilic
CARD/CARD ( Caspase Recruitment Domain ) interaction is critical for the activation of caspases downstream of mitochondrial damage in apoptosis
Pathan et al., J Biol Chem 2001
(Neoplasms) :
TUCAN interferes with binding of Apaf1 to procaspase-9 and
suppresses caspase activation induced by the Apaf1 activator, cytochrome c. Overexpression of TUCAN in cells by stable or transient transfection inhibits apoptosis and caspase activation induced by Apaf1/caspase-9 dependent stimuli, including Bax, VP16, and staurosporine, but not by Apaf1/caspase-9 independent stimuli, Fas and granzyme B
Shiozaki et al., Proc Natl Acad Sci U S A 2002
:
Oligomerization and activation of
caspase-9 ,
induced by Apaf-1
CARD
Chamaillard et al., Cell Microbiol 2003
(Bacterial Infections...) :
NBS-LRR proteins are characterized by three structural domains : a C-terminal leucine-rich repeat ( LRR ) domain able to sense a microbial motif, an intermediary nucleotide binding site (NBS) essential for the oligomerization of the molecule that is necessary for the signal transduction induced by different N-terminal effector motifs, such as a pyrin domain ( PYD ), a
caspase activating and recruitment domain (
CARD ) or a baculovirus inhibitor of apoptosis protein repeat ( BIR ) domain
Checinska et al., BMC cancer 2006
(Carcinoma, Non-Small-Cell Lung) :
Proteins interaction assays, and RNA interference in combination with cell viability and apoptosis assays were used to investigate the
involvement of
TUCAN in inhibition of
caspase-9 and chemosensitivity NSCLC ... Furthermore, RNA interference mediated down-regulation of
TUCAN did not
restore cisplatin induced
caspase-9 activation or affect cisplatin sensitivity in NSCLC cells
Ko et al., Am J Hum Genet 2009
(Bacterial Infections) :
A loss-of-function allele of
CARD8 , a reported
inhibitor of the proinflammatory protease
caspase-1 , was associated with increased cell death in vitro ( p = 0.013 )