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CASP12 — RIPK1
Text-mined interactions from Literome
Martinet et al., Autophagy 2006
(Atherosclerosis) :
This finding suggests that
caspase inhibition
activates RIP1 which in turn initiates autophagy, although other explanations should be taken into account
Wang et al., Cell 2008
:
RIPK1 is
critical for
caspase-8 activation induced by Smac mimetic but dispensable for that triggered by cycloheximide
Morgan et al., J Immunol 2009
:
Membrane bound Fas ligand
requires RIP1 for efficient activation of
caspase-8 within the death inducing signaling complex
Gentle et al., J Biol Chem 2011
:
After receptor ligation,
RIPK1 not only modulates activation of both canonical and NIK dependent NF-?B, but also
regulates caspase-8 activation and cell death ... After receptor ligation,
RIPK1 not only modulates activation of both canonical and NIK dependent NF-?B, but also
regulates caspase-8 activation and cell death
Löder et al., Leukemia 2012
(Precursor Cell Lymphoblastic Leukemia-Lymphoma) :
Similarly, inhibition of
RIP1 kinase activity by Necrostatin-1 or blockage of TNFa by Enbrel
inhibits IAP inhibitor- and AraC triggered interaction of RIP1, FADD and
caspase-8 and apoptosis
Duprez et al., Immunity 2011
(Cecal Diseases...) :
An additional switch decides, depending on the cellular context, between
caspase dependent apoptosis and
RIP kinase ( RIPK ) -mediated necrosis, also termed necroptosis
Basit et al., J Biol Chem 2012
(Rhabdomyosarcoma) :
Importantly, knockdown of RIP1 by RNA interference prevented the formation of the
RIP1·FADD·caspase-8 complex and inhibited subsequent
activation of
caspase-8 , -9, and -3 ; loss of mitochondrial membrane potential ; and apoptosis upon treatment with IAP inhibitor and lexatumumab
Kaczmarek et al., Immunity 2013
(Bacterial Infections...) :
Regulated necrosis, termed necroptosis, is negatively regulated by
caspase-8 and is
dependent on the kinase activity of
RIPK1 and RIPK3