Any feedback?
Literature summary for 3.4.22.64 extracted from
- Revisiting caspase-11 function in host defense (2013), Cell Host Microbe, 14, 9-14.
Activating Compound
| 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(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Casp11 | Mus musculus |
Protein Variants
| 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
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Mus musculus | 5829 | - |
| cytosol | - |
Homo sapiens | 5829 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
gene Casp11 | - |
Source Tissue
| 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
| Subunits | Comment | Organism |
|---|---|---|
| dimer | activation through dimerization | Mus musculus |
| dimer | activation through dimerization | Homo sapiens |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Mus musculus | bacterial lipopolysaccharide stimulation of caspase-11 expression in several mouse tissues, particularly in the spleen | up |
General Information
| 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
