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Literature summary for 3.4.22.64 extracted from

  • Ng, T.M.; Monack, D.M.
    Revisiting caspase-11 function in host defense (2013), Cell Host Microbe, 14, 9-14.
    View publication on PubMed
Search for more literature for 3.4.22.64

Activating Compound

Activating Compound Comment Organism Structure
cholera toxin B a caspase-11-activating toxin Homo sapiens
cholera toxin B a caspase-11-activating toxin Mus musculus
additional information activation through dimerization. Signaling pathways involved in caspase-11 activation, overview Homo sapiens
additional information activation through dimerization. Signaling pathways involved in caspase-11 activation, overview Mus musculus

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
-
 Homo sapiens 5829
-
cytosol
-
 Mus musculus 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 Homo sapiens
dimer activation through dimerization Mus musculus

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 Homo sapiens
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
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-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
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