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Literature summary for 3.4.22.64 extracted from

  • Akuma, D.C.; Wodzanowski, K.A.; Schwartz Wertman, R.; Exconde, P.M.; Vazquez Marrero, V.R.; Odunze, C.E.; Grubaugh, D.; Shin, S.; Taabazuing, C.; Brodsky, I.E.
    Catalytic activity and autoprocessing of murine caspase-11 mediate noncanonical inflammasome assembly in response to cytosolic LPS (2024), eLife, 13, e83725.
    View publication on PubMed
Search for more literature for 3.4.22.64

Activating Compound

Activating Compound Comment Organism Structure
LPS cytosolic LPS induces Casp11 speck formation. Binding of bacterial LPS to its cytosolic sensor, caspase-11 (Casp11), promotes Casp11 aggregation within a high-molecular-weight complex and activation of caspase-11 catalytic activity Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
gene CASP4, recombinant expression of 2xFLAG-tagged wild-type and mutant enzymes in HEK-293T cells Mus musculus

Protein Variants

Protein Variants Comment Organism
C254A site-directed mutagenesis, the catalytically inactive mutant shows highly reduced speck formation, catalytically deficient Casp11 lacks the ability to oligomerize autonomously Mus musculus
C254A/D285A site-directed mutagenesis, an inactive, IDL-uncleavable Casp11 mutant Mus musculus
D285A site-directed mutagenesis, mutation of the IDL cleavage site, the non-cleavable mutant shows highly reduced speck formation Mus musculus
additional information recombinant expression of fluorescently labeled Casp11 in macrophages reveals that cytosolic LPS induces Casp11 speck formation in transformed HEK-293T cells. Both catalytic activity and autoprocessing are required for Casp11 speck formation in an ectopic expression system, and processing of Casp11 via ectopically expressed TEV protease is sufficient to induce Casp11 speck formation. Wild-type caspase-11 recruits catalytically inactive caspase-11 to speck complexes independently of trans-processing Mus musculus

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
gasdermin D + H2O Mus musculus
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P70343 cf. caspase-4, EC 3.4.22.57
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme needs to be self-cleaved to become activated, autoprocessing at the interdomain linker. Enzyme mutant D285A is non-cleavable. Caspase-11 autoprocessing mediates noncanonical inflammasome assembly Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
macrophage bone marrow-derived Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gasdermin D + H2O
-
 Mus musculus ?
-
 ?

Subunits

Subunits Comment Organism
dimer inducible dimerization activates caspase-11. Formation of a functional Casp11 inflammasome supramolecular organizing center (SMOC) involves additional steps beyond inducible dimerization, overview Mus musculus
additional information caspase-11 catalytic activity and autoprocessing at the interdomain linker are required for spontaneous caspase-11 oligomerization in recombinant HEK293T cells Mus musculus

Synonyms

Synonyms Comment Organism
CASP11
-
 Mus musculus

General Information

General Information Comment Organism
malfunction wild-type caspase-11 recruits catalytically inactive caspase-11 to speck complexes independently of trans-processing. Catalytically inactive enzyme mutant and non-cleavable enzyme mutant show highly reduced speck formation Mus musculus
metabolism caspases-1 and -11 are inflammatory caspases that are recruited into inflammasome supramolecular organizing centers (SMOCs), which mediate the effector function of the PRR signaling pathway in response to microbial infection or pathologic stimulus, in response to the cytosolic presence of pathogen-derived signals or molecules. Caspase-11 autoprocessing mediates noncanonical inflammasome assembly, overview Mus musculus
physiological function inflammasomes recruit caspases to undergo proximity-induced autoprocessing into an enzymatically active form that cleaves downstream targets. Binding of bacterial LPS to its cytosolic sensor, caspase-11 (Casp11), promotes Casp11 aggregation within a high-molecular-weight complex known as the noncanonical inflammasome, where it is activated to cleave gasdermin D and induce pyroptosis. Casp11 catalytic activity and autoprocessing are required for Casp11 to form LPS-induced specks in macrophages and both catalytic activity and autoprocessing are required for Casp11 speck formation downstream of homodimerization in an ectopic expression system, and processing of Casp11 via ectopically expressed TEV protease is sufficient to induce Casp11 speck formation, detailed overview. Caspase-11 autoprocessing mediates noncanonical inflammasome assembly Mus musculus