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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.