◀ Back to CASP2
CASP2 — PIDD
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
PIDD
—
CASP2
(physical association, affinity chromatography technology)
Tinel et al., Science 2004*
-
IRef Biogrid Interaction:
PIDD
—
CASP2
(physical association, affinity chromatography technology)
Janssens et al., Cell 2005*
-
IRef Biogrid Interaction:
PIDD
—
CASP2
(physical association, affinity chromatography technology)
Logette et al., Cell Death Differ 2011
-
IRef Hprd Interaction:
PIDD
—
CASP2
(in vivo)
Tinel et al., Science 2004*, Vakifahmetoglu et al., Oncogene 2006*
-
IRef Hprd Interaction:
Complex of CRADD-CASP2-CRADD-PIDD-PIDD-CRADD-CASP2-PIDD-CASP2
(in vivo)
Vakifahmetoglu et al., Oncogene 2006*
Text-mined interactions from Literome
Tinel et al., Science 2004
:
Increased
PIDD expression
resulted in spontaneous activation of
caspase-2 and sensitization to apoptosis by genotoxic stimuli
Ren et al., Proc Natl Acad Sci U S A 2005
(Embryo Loss) :
This apoptosis is associated with up-regulation and nuclear localization of the tumor suppressor p53 and activation of mitochondrial apoptosis, which includes up-regulation of Bax, Bak, and
Pidd , translocation of Bax and caspase-2 onto mitochondria, release of cytochrome c and apoptosis inducing factor, and
activation of
caspase-9 and caspase-3
Manzl et al., J Cell Biol 2009
:
Because loss of either
PIDD or its adapter molecule RAIDD did not
affect subcellular localization, nuclear translocation, or
caspase-2 activation in high molecular weight complexes, we suggest that at least one alternative PIDDosome independent mechanism of caspase-2 activation exists in mammals in response to DNA damage
Oliver et al., Mol Cell 2011
:
Caspase-2 is
activated by the p53 target gene product
PIDD ( also known as LRDD ) in a complex called the Caspase-2-PIDDosome ...
PIDD induced
Caspase-2 directly cleaves the E3 ubiquitin ligase Mdm2 at Asp 367, leading to loss of the C-terminal RING domain responsible for p53 ubiquitination