Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cholera toxin B | a caspase-11-activating toxin | Mus musculus | |
cholera toxin B | a caspase-11-activating toxin | Homo sapiens | |
additional information | activation through dimerization. Signaling pathways involved in caspase-11 activation, overview | Mus musculus | |
additional information | activation through dimerization. Signaling pathways involved in caspase-11 activation, overview | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
gene Casp11 | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | recombination and segregation of the nonfunctional Casp11 gene away from the Casp1-/- locus is nearly impossible because Casp1 and Casp11 occur only about 1500 bp apart on chromosome 9 in 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 | - |
gene Casp11 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
bone marrow-derived macrophage | - |
Mus musculus | - |
spleen | the highest expression levels of murine Casp11 gene are observed in spleens | Mus musculus | - |
Subunits | Comment | Organism |
---|---|---|
dimer | activation through dimerization | Mus musculus |
dimer | activation through dimerization | Homo sapiens |
Organism | Comment | Expression |
---|---|---|
Mus musculus | bacterial lipopolysaccharide stimulation of caspase-11 expression in several mouse tissues, particularly in the spleen | up |
General Information | Comment | Organism |
---|---|---|
malfunction | upon infection with Salmonella typhimurium, the level of pro-interleukin-1beta maturation in bone marrow derived macrophages is reduced in the absence of caspase-11 | Mus musculus |
metabolism | apoptosis is triggered by the initiator caspases, caspase-2, -8, -9, and -10, which subsequently activate the executioner caspases, caspase-3, -6, and -7 | Mus musculus |
metabolism | apoptosis is triggered by the initiator caspases, caspase-2, -8, -9, and -10, which subsequently activate the executioner caspases, caspase-3, -6, and -7 | Homo sapiens |
additional information | caspase-1, -2, -4, -9, and -11 have particularly long pro-domains that contain either death effector domains (DED) or caspase recruitment domains (CARD), which are thought to confer specificity of activation since they mediate interactions with other DED- and CARD-containing adaptor proteins. Association with these adaptor proteins likely nucleates caspases, increasing their local concentration. This nucleation can favor activation through dimerization | Homo sapiens |
additional information | caspase-11 cooperatively interacts with actin-interacting protein to activate cofilin-dependent actin depolymerization leading to increased splenocyte migration, caspase-11-mediated actin depolymerization appears to be independent of its enzymatic activity. Caspase-1, -2, -4, -9, and -11 have particularly long pro-domains that contain either death effector domains (DED) or caspase recruitment domains (CARD), which are thought to confer specificity of activation since they mediate interactions with other DED- and CARD-containing adaptor proteins. Association with these adaptor proteins likely nucleates caspases, increasing their local concentration. This nucleation can favor activation through dimerization | Mus musculus |
physiological function | caspase-11 is required for cofilin phosphorylation. Caspase-11-dependent cell death and interleukin-1beta secretion can only be detected in vitro in the absence of a NAIP/NLRC4 stimulus, e.g. flagellin. Caspase-11 is required for the release of the alarmins, interleukin-1alpha and HMGB1. The role of caspase-11 in pro-interleukin-18 and pro-interleukin-1beta maturation is dependent on NLRP3/ASC/CASP1 inflammasomes. Pro-inflammatory caspases play important roles in innate immunity. Caspase-11 contributes to host defenses against pathogen invasion. Caspase-11 functions and mechanisms of activation, overview | Mus musculus |
physiological function | caspase-11-dependent cell death and interleukin-1beta secretion can only be detected in vitro in the absence of a NAIP/NLRC4 stimulus, e.g. flagellin. Caspase-11 is required for the release of the alarmins, interleukin-1alpha and HMGB1. The role of caspase-11 in pro-interleukin-18 and pro-interleukin-1beta maturation is dependent on NLRP3/ASC/CASP1 inflammasomes. Pro-inflammatory caspases play important roles in innate immunity, analysis of mechanisms by which caspase-11 contributes to host defense. Caspase-11 functions and mechanisms of activation, implications for human disease, overview | Homo sapiens |