Protein Variants | Comment | Organism |
---|---|---|
additional information | all Casp1-/- mouse strains generated from 129 embryonic stem cells also lack caspase-11 due to a 5-bp deletion in the caspase-11 locus that causes loss of the catalytic domain. As the caspase-11 and caspase-1 loci are located physically close together, the mutations do not segregate during backcrossing, leading to double mutant mice | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Mus musculus | 5829 | - |
cytosol | - |
Homo sapiens | 5829 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | TRIF is required for the processing of procaspase-11 into the cleaved caspase-11 forms | Homo sapiens |
proteolytic modification | TRIF is required for the processing of procaspase-11 into the cleaved caspase-11 forms. IFNs or lipopolyaccharides alone are not sufficient to trigger caspase-11 processing, but an unidentified factor derived from live Gram-negative bacteria is required, which is likely a mechanism to ensure that inflammatory responses do not proceed in the absence of active infection | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
macrophage | - |
Mus musculus | - |
macrophage | - |
Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
Ich-3 | - |
Mus musculus |
Organism | Comment | Expression |
---|---|---|
Mus musculus | induction of procaspase-11 expression is delayed in Myd88-/- macrophages infected with DELTAFlag Salmonella typhimurium, although procaspase-11 processing itself remains intact | additional information |
General Information | Comment | Organism |
---|---|---|
malfunction | defects in the IFN-alpha/beta, but not IFN-gamma, pathways render macrophages severely impaired in processing of caspase-11 following infection with Salmonella typhimurium, EHEC or Citrobacter rodentium, while exogenous IFN-beta rescues caspase-11 processing in Trif-/- macrophages. The absence of the TRIF-IFNAR pathway abolishes both the expression and activation of caspase-11, and treatment of Trif-/- macrophages with IFN-beta or IFN-gamma restores both the precursor and cleaved forms of caspase-11 | Mus musculus |
physiological function | mechanisms and implications of caspase-11-mediated noncanonical inflammasome activation, importance of this pathway in regulating host defense against intracellular bacterial pathogens. The pathway engages caspase-11 to trigger both caspase-1-dependent and -independent production of the inflammatory cytokines IL-1beta, IL-18, and IL-1alpha, as well as to promote pyroptosis, a form of genetically programmed cell death that is associated with the release of such cytokines. Caspase-11 is regulated in response to extracellular stimuli, such as lipopolysaccharide and interferons | Homo sapiens |
physiological function | mechanisms and implications of caspase-11-mediated noncanonical inflammasome activation, importance of this pathway in regulating host defense against intracellular bacterial pathogens. The pathway engages caspase-11 to trigger both caspase-1-dependent and -independent production of the inflammatory cytokines IL-1beta, IL-18, and IL-1alpha, as well as to promote pyroptosis, a form of genetically programmed cell death that is associated with the release of such cytokines. Caspase-11 is regulated in response to extracellular stimuli, such as lipopolysaccharide and interferons. Regulation of caspase-11 expression, models of activation, and caspase-11 effector functions, overview. Role of caspase-11 in pyroptosis, caspase-11 directly controls the activation of the effector caspases 3 and 7 of the apoptotic pathway independent of caspase-1 | Mus musculus |