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Literature summary for 3.4.22.64 extracted from

  • Shin, S.; Brodsky, I.E.
    Caspase-11: the noncanonical guardian of cytosolic sanctity (2013), Cell Host Microbe, 13, 243-245.
    View publication on PubMed
Search for more literature for 3.4.22.64

Activating Compound

Activating Compound Comment Organism Structure
additional information the adaptor protein TRIF upregulates procaspase-11 expression, and this upregulation is required for caspase-11 processing and activation. Lipopolysaccharide treatment or type I IFN treatment alone does not cause caspase-11-dependent cell death Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information all Casp1-/- mice also lack caspase-11, due to the generation of the Casp1-/- line in the 129 mouse strain background, which express a mis-spliced and truncated version of the Casp11 messenger RNA Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Mus musculus 5829
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
 gene Casp11
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the adaptor protein TRIF upregulates procaspase-11 expression, and this upregulation is required for caspase-11 processing and activation Mus musculus

Expression

Organism Comment Expression
Mus musculus Lipopolysaccharide treatment or type I IFN treatment alone does not cause caspase-11-dependent cell death additional information
Mus musculus type I IFN signaling is sufficient to induce caspase-11 upregulation and processing. The adaptor protein TRIF upregulates procaspase-11 expression, and this upregulation is required for caspase-11 processing and activation up

General Information

General Information Comment Organism
malfunction all Casp1-/- mice also lack caspase-11, due to the generation of the Casp1-/- line in the 129 mouse strain background, which express a mis-spliced and truncated version of the Casp11 messenger RNA Mus musculus
metabolism Gram-negative bacteria and certain pore-forming toxins induce a caspase-11-dependent noncanonical inflammasome that contributes to NLRP3-dependent interleukin-1beta release and also triggers NLRP3- and caspase-1-independent cell death and interleukin-1alpha release Mus musculus
physiological function activated caspase-11 triggers cell death, caspase-11 is essential for the induction of endotoxic shock in vivo Mus musculus