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Literature summary for 3.4.22.64 extracted from

  • Case, C.L.; Kohler, L.J.; Lima, J.B.; Strowig, T.; de Zoete, M.R.; Flavell, R.A.; Zamboni, D.S.; Roy, C.R.
    Caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila (2013), Proc. Natl. Acad. Sci. USA, 110, 1851-1856.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
additional information caspase-11 is activated by a cytosolic sensing mechanism that detects bacterial-derived signals delivered into the host cytosol through the type IV secretion apparatus. Caspase-11 activation by Legionella pneumophila has distinct kinetic and molecular parameters, overview. Caspase-11 activation requires upstream protein(s) capable of sensing a microbial or endogenous danger signal. Caspase-11 requires type I IFN production mediated by TRIF-dependent TLR signaling. And caspase-1 is dispensable for caspase-11-dependent pyroptosis induced by Legionella pneumophila Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Mus musculus C57BL/6
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Source Tissue

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

General Information Comment Organism
physiological function caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila. NLRP3 and ASC are both required for caspase-1 activation through the caspase-11-dependent pathway induced by Legionella pneumophila, caspase-11 is required for NAIP/NLRC4-independent pyroptosis Induced by Legionella pneumophila Mus musculus