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PMID: 17967410, 12796777, 1279199716870615 NOD1 recognizes the dipeptide gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), which is produced by most Gram-negative and specific Gram-positive bacteria.

PMID: 17967410, 12527755, 12514169 In contrast, NOD2 is activated by muramyl dipeptide (MDP), a component of virtually all types of PGN.

PMID: 17967410 The current model proposes that when PAMPs are sensed by the C-terminal LRRs, the molecule undergoes conformational rearrangements triggering oligomerization via the NOD domain.

PMID: 17967410 The current model proposes that when PAMPs are sensed by the C-terminal LRRs, the molecule undergoes conformational rearrangements triggering oligomerization via the NOD domain.

PMID: 17967410, 10329646, 11087742 Direct or indirect ligand recognition by the LRRs of NOD1 and NOD2 induces the recruitment of RICK through homotypic CARD interactions.

PMID: 17967410, 10329646, 11087742 Direct or indirect ligand recognition by the LRRs of NOD1 and NOD2 induces the recruitment of RICK through homotypic CARD interactions.

PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.

PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.

PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.

PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.

PMID: 17967410 The NLR proteins NOD1 and NOD2 sense intracellular iE-DAP and MDP, respectively, leading to recruitment of the adaptor proteins RICK and CARD9. PMID: 17967410, 17187069 The CARD-containing adaptor protein CARD9 was found to be important for the activation of p38 and JNK downstream of NOD2, although it was dispensable for NF-kappaB activation

Indirect

PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex.

Indirect

PMID: 17967410, 15620648, 17348859 This CARD-containing serine-threonine kinase directly binds and promotes K63-type polyubiquitylation of the regulator IKK-gamma and activation of the kinase TAK1 a prerequisite for activation of the IKK complex. PMID: 17967410, 17187069 The CARD-containing adaptor protein CARD9 was found to be important for the activation of p38 and JNK downstream of NOD2, although it was dispensable for NF-kappaB activation

Indirect

PMID: 17967410, 11463746, 15692051, 14560001 In addition to the NF-kappaB pathway, NOD1 or NOD2 stimulation results in the activation of the MAP kinases p38, ERK, and JNK. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410, 11463746, 15692051, 14560001 In addition to the NF-kappaB pathway, NOD1 or NOD2 stimulation results in the activation of the MAP kinases p38, ERK, and JNK. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410, 11463746, 15692051, 14560001 In addition to the NF-kappaB pathway, NOD1 or NOD2 stimulation results in the activation of the MAP kinases p38, ERK, and JNK. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410 These events result in the degradation of the NF-kappaB inhibitor IkappaB-alpha and the subsequent translocation of NF-kappaB to the nucleus, where transcription of NF-κB-dependent target genes occurs.

PMID: 17967410 These events result in the degradation of the NF-kappaB inhibitor IkappaB-alpha and the subsequent translocation of NF-kappaB to the nucleus, where transcription of NF-κB-dependent target genes occurs. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410 These events result in the degradation of the NF-kappaB inhibitor IkappaB-alpha and the subsequent translocation of NF-kappaB to the nucleus, where transcription of NF-κB-dependent target genes occurs. PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.

PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.

Indirect

PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.

Indirect

PMID: 17967410 Extracellular PAMPs are recognized by TLRs, which signals through MyD88, IRAK proteins, and TRAF members.

Indirect

PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

Indirect

PMID: 17967410, 16513653 Moreover, H. pylori-induced production of beta-defensins was abolished in Nod1−/− mice.

Indirect

PMID: 17967410 Recognition of PAMPs by TLRs induces synthesis of the IL-1beta precursor through activation of NF-kappaB.

PMID: 17967410 These results demonstrate that TLR5 and Ipaf represent two flagellin receptors that have evolved to control distinct signaling pathways (NF-kappaB activation and caspase-1 activation, respectively) when the host is infected with Salmonella or Legionella.

PMID: 17967410, 16984919, 16648852, 16648853 Flagellin was identified as the bacterial molecule that is sensed by Ipaf, and flagellin-deficient bacteria are compromised in their capability to induce caspase-1 activation and secretion of IL-1beta. PMID: 17967410, 16984919, 16648852, 16648853 The finding that recombinant purified flagellin induces Ipaf-dependent caspase-1 activation when delivered directly into the cytosol indicates that the cytosolic presence of flagellin is essential and sufficient for Ipaf activation.

Indirect

PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

Indirect

PMID: 17967410 The subsequent activation of NF-kappaB and MAP kinases results in the transcriptional upregulation of proinflammatory genes.

PMID: 17967410 The inflammasome adaptor ASC is required for recruitment of caspase-1, although its role in the Nalp1b inflammasome needs to be confirmed.

PMID: 17967410 Ipaf rapidly activates caspase-1 when it senses the intracellular pathogens Salmonella typhimurium or Legionella pneumophila. PMID: 17967410, 16984919, 16648852, 16648853 Flagellin was identified as the bacterial molecule that is sensed by Ipaf, and flagellin-deficient bacteria are compromised in their capability to induce caspase-1 activation and secretion of IL-1beta.

Indirect

PMID: 17967410 These results demonstrate that TLR5 and Ipaf represent two flagellin receptors that have evolved to control distinct signaling pathways (NF-kappaB activation and caspase-1 activation, respectively) when the host is infected with Salmonella or Legionella.

Indirect

Indirect

PMID: 17967410, 16984919, 16648852, 16648853 Flagellin was identified as the bacterial molecule that is sensed by Ipaf, and flagellin-deficient bacteria are compromised in their capability to induce caspase-1 activation and secretion of IL-1beta. PMID: 17967410 Active caspase-1 processes the IL-1beta precursor into the mature cytokine, which is secreted through an unknown mechanism. PMID: 17967410, 15190255, 12191486 This bipartite CARD-PYD protein bridges the association of caspase-1 to the NLR proteins Nalp1 and Cryopyrin in the inflammasomes and therefore plays a major role in the activation of caspase-1 and the subsequent maturation of the inflammatory cytokines IL-1beta and IL-18. PMID: 17967410, 16407888 Bacterial RNA and the imidazoquinoline compounds R837 and R848 alone induce IL-1beta secretion, but a brief pulse with ATP markedly enhances caspase-1 activation and IL-1beta maturation.

PMID: 17967410, 17349957 Although there is no evidence for a physical interaction between cryopyrin and microbial molecules, purified NALP1 has been shown to mediate caspase-1 activation in response to MDP.

PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.

PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.

PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.\ PMID: 17967410, 17418785 Recently, Reed and colleagues showed that the antiapoptotic Bcl-2 members Bcl-2 and Bcl-XL specifically interact with human Nalp1 and prevent Nalp1-mediated caspase-1 activation.

PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.

PMID: 17967410, 17418785 Recently, Reed and colleagues showed that the antiapoptotic Bcl-2 members Bcl-2 and Bcl-XL specifically interact with human Nalp1 and prevent Nalp1-mediated caspase-1 activation.

PMID: 17967410, 17418785 Recently, Reed and colleagues showed that the antiapoptotic Bcl-2 members Bcl-2 and Bcl-XL specifically interact with human Nalp1 and prevent Nalp1-mediated caspase-1 activation.

PMID: 17967410 Salmonella and Legionella flagellin are sensed by Ipaf, whereas mouse Nalp1b recognizes anthrax lethal toxin.

PMID: 17967410, 12191486 The prodomain of the prototypical inflammatory caspase-1 encodes a CARD, also present in the C terminus of NOD1, NOD2, and RICK. Caspase-1 is recruited to large multiprotein complexes known as “inflammasomes” through homotypic interactions with the CARD motif in the adaptor ASC.

PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.

PMID: 17967410, 15030775, 17349957 In contrast to mouse Nalp1b, human NALP1 interacts with ASC and the adaptor protein CARDINAL to recruit and activate the inflammatory caspase-1 and -5.

PMID: 17967410, 17008311, 17433728, 16407890 Cryopyrin and the inflammasome adaptor ASC are required for caspase-1 activation in response to microbial products with diverse molecular structures such as LPS, peptidoglycan, and lipoteichoic acid when combined with millimolar concentrations of ATP.

PMID: 17967410, 17008311, 17433728, 16407890 Cryopyrin and the inflammasome adaptor ASC are required for caspase-1 activation in response to microbial products with diverse molecular structures such as LPS, peptidoglycan, and lipoteichoic acid when combined with millimolar concentrations of ATP.

PMID: 17967410, 17008311, 17433728, 16407890 Cryopyrin and the inflammasome adaptor ASC are required for caspase-1 activation in response to microbial products with diverse molecular structures such as LPS, peptidoglycan, and lipoteichoic acid when combined with millimolar concentrations of ATP.

Indirect

PMID: 17967410, 17433728 Nevertheless, TLRs are still essential for NF-kappaB-dependent production of pro-IL-1beta.

Indirect

PMID: 17967410, 17433728, 15507117 Indeed, the TLR4 ligand LPS induced activation of caspase-1 in macrophages deficient in MyD88, TRIF, or TLR4.

PMID: 17967410 In this model, pannexin-1 delivers bacterial molecules into the cytosol where they are sensed by cryopyrin. PMID: 17967410, 17036048 Notably, pannexin-1 was found to be critical for caspase-1 activation and IL-1beta secretion in LPS-stimulated macrophages pulsed with ATP.

PMID: 17067410 Another NLR protein, the CIITA transcription factor, is required for the transcription of genes encoding MHC II, whereas the NLR family members Nalp1 and Cryopyrin recruit the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD) to activate caspase-1.

PMID: 17067410 Another NLR protein, the CIITA transcription factor, is required for the transcription of genes encoding MHC II, whereas the NLR family members Nalp1 and Cryopyrin recruit the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD) to activate caspase-1.

PMID: 17967410 Cryopyrin/Nalp3 mediates caspase-1 activation in response to a wide variety of microbial components and the endogenous danger signal uric acid. PMID: 17967410 The latter is more consistent with the fact that cryopyrin induces caspase-1 activation in response to a plethora of bacterial ligands in the presence of ATP.

Indirect

PMID: 17967410 Bacteria and bacterial products enter the cytosol via pore-forming toxins, type III or IV secretion systems, or ATP-mediated activation of the pannexin-1 pore.

Indirect

PMID: 17967410 Francisella induce ASC-dependent caspase-1 activation through an NLR, the identity of which is unknown.

Indirect

PMID: 17967410, 15190255, 12191486 This bipartite CARD-PYD protein bridges the association of caspase-1 to the NLR proteins Nalp1 and Cryopyrin in the inflammasomes and therefore plays a major role in the activation of caspase-1 and the subsequent maturation of the inflammatory cytokines IL-1beta and IL-18.

Indirect

Indirect

PMID: 17967410, 16407888 Bacterial RNA and the imidazoquinoline compounds R837 and R848 alone induce IL-1beta secretion, but a brief pulse with ATP markedly enhances caspase-1 activation and IL-1beta maturation.

Indirect

Indirect

PMID: 17967410, 16407888 Bacterial RNA and the imidazoquinoline compounds R837 and R848 alone induce IL-1beta secretion, but a brief pulse with ATP markedly enhances caspase-1 activation and IL-1beta maturation.

Indirect

PMID: 17967410, 17491021 Stimulation of the P2X7 receptor with ATP induces K+ efflux, a signal that has been implicated in cryopyrin-mediated caspase-1 activation.

Indirect

PMID: 17967410, 17121814 ATP triggers the potassium-selective channel of the purinergic P2X7 receptor to open.

Indirect

Indirect

PMID: 17967410 Bacteria and bacterial products enter the cytosol via pore-forming toxins, type III or IV secretion systems, or ATP-mediated activation of the pannexin-1 pore. PMID: 17967410, 17240370, 17121814, 17036048 Recent studies have revealed that the rapid activation of P2X7 receptor is followed by the gradual opening of a larger pore attributed to the hemichannel pannexin-1, which is recruited upon P2X7 receptor activation.

Indirect

Indirect

PMID: 17967410, 16407889 The finding that monosodium urate (MSU) and calcium pyrophosphate dehydrate (CPPD) crystals require cryopyrin, but not ATP, to activate caspase-1 suggests a role for the cryopyrin inflammasome in the pathogenesis of gout and pseudogout.

Indirect

Indirect

PMID: 17967410, 16407889 The finding that monosodium urate (MSU) and calcium pyrophosphate dehydrate (CPPD) crystals require cryopyrin, but not ATP, to activate caspase-1 suggests a role for the cryopyrin inflammasome in the pathogenesis of gout and pseudogout.