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RELA — RIPK2

Pathways - manually collected, often from reviews:

• KEGG Tuberculosis: RIPK2 → NFKB1/RELA (protein-protein, activation)

Text-mined interactions from Literome

Chin et al., Nature 2002 (Listeriosis...) : Rip2-deficient macrophages infected with L. monocytogenes or treated with lipopolysaccharide (LPS) have decreased activation of NF-kappaB, whereas dominant negative Rip2 inhibited NF-kappaB activation mediated by Toll-like receptor 4 and Nod1
Ruefli-Brasse et al., J Biol Chem 2004 : Together these data define an important role for Rip2 in TCR induced NF-kappaB activation and T-cell function and highlight the significance of post-translational modification of Bcl10 by Rip2 in T-cell signaling
Lamkanfi et al., J Biol Chem 2004 (MAP Kinase Signaling System) : We demonstrate that caspase-1 interacts with RIP2 and that dominant negative forms of RIP2 and IkappaB kinase complex-beta inhibit caspase-1 mediated NF-kappaB activation ... These data demonstrate that caspase-1 contributes to inflammation by two distinct pathways : proteolysis of pro-IL-1beta, and RIP2 dependent activation of NF-kappaB and p38 MAPK mediated by the caspase recruitment domain
Lamkanfi et al., J Biol Chem 2004 : Unlike COP/Pseudo-ICE and procaspase-1, INCA does not interact with RIP2 and does not induce NF-kappaB activation
Abbott et al., Curr Biol 2004 (Crohn Disease) : Lastly, we show functionally that RIP2 induced ubiquitinylation of NEMO is at least in part responsible for RIP2 mediated NF-kB activation
Li et al., J Cell Sci 2005 : Overexpression of TRIP6 potentiates RIP2 mediated NF-kappaB activation in a dose dependent manner
Sarkar et al., J Immunol 2006 : Receptor interacting protein-2 (RIP2) is a caspase recruitment domain ( CARD ) -containing kinase that interacts with caspase-1 and plays an important role in NF-kappaB activation ... This RIP2 induced NF-kappaB activity and caspase-1 binding was inhibited in a dose dependent fashion by ASC ... These data suggest that ASC may direct caspase-1 away from RIP2 mediated NF-kappaB activation , toward caspase-1 mediated processing of proIL-1beta by interfering with the RIP2 caspase-1 interaction
Dufner et al., Mol Cell Biol 2008 : RIP2 mediates NF-kappaB activation induced by the intracellular nucleotide binding oligomerization domain ( NOD ) receptors that sense bacterial peptidoglycan
Fukazawa et al., PLoS Pathog 2008 (Dysentery, Bacillary) : GEF-H1 interacts with NOD1 and is required for RIP2 dependent NF-kappaB activation by H-Ala-D-gammaGlu-DAP ( gammaTriDAP )
Krieg et al., Mol Immunol 2009 : RIP2 promotes NF-kappaB activation as well as activation of the MAPKs JNK, ERK1/2 and p38 MAPK, thereby playing an emergent role in the innate immune response and NOD signaling
Hideshima et al., Blood 2009 (Multiple Myeloma) : Bortezomib triggered phosphorylation of IkappaB kinase ( IKKbeta ) and its upstream receptor interacting protein 2, whereas IKKbeta inhibitor MLN120B blocked bortezomib induced IkappaBalpha down-regulation and NF-kappaB activation, indicating receptor interacting protein 2/IKKbeta signaling plays crucial role in bortezomib induced NF-kappaB activation
Tao et al., Curr Biol 2009 (Crohn Disease) : We also show that NOD2 can bind polyubiquitinated RIP2 and that whereas ITCH E3 ligase activity is required for optimal NOD2 : RIP2 induced p38 and JNK activation, ITCH inhibits NOD2 : RIP2 induced nuclear factor kappa B (NFkappaB) activation
Yin et al., Mol Cell Biochem 2010 : Two mechanistically distinct inhibitors of NF-kappaB signaling, sulfasalazine ( NF-kappaB inhibitor ) and WY-14643 [ PPAR alpha ( peroxisome proliferator activated receptor alpha ) agonist ] that interfere with the transcription factor RELA ( p65 ), suppressed TNF-alpha induced RIP-2 gene expression, which indicated that NF-kappaB signaling was involved in the cytokine induced transcriptional activation of RIP-2 gene expression ... NF-kappaB mediated regulation of RIP-2 gene and protein expression suggests an additional step in the regulation of NF-kappaB function as RIP-2 has been shown to positively modulate NF-kappaB by binding IKK gamma ( I kappaB kinase gamma ), a component of the IKK complex ... These findings support a positive feed-forward mechanism of NF-kappaB regulation that involves NF-kappaB dependent induction of RIP-2 transcription and a subsequent increase in RIP-2 protein levels in response to inflammatory cytokines
Oh et al., J Pharmacol Exp Ther 2011 (Inflammation...) : In activated human mast cells, the receptor interacting protein 2 (RIP2) , I?B kinase ( IKK ) -ß, nuclear factor-?B ( NF-?B ) /RelA, and caspase-1 activation were increased, but increased RIP2, IKK-ß, NF-?B/RelA , and caspase-1 activation were inhibited by the treatment of IPT
McCarthy et al., J Biol Chem 1998 : RIP2 is a novel NF-kappaB activating and cell death inducing kinase