EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.64 | phosphoprotein |
L-adrenaline binds ADRA2B, activating PKA. Activated PKA facilitates caspase-11 phosphorylation |
772221 |
| 3.4.22.64 | proteolytic modification |
caspase-11 performs LPS-induced autoprocessing to activate itself. Mutations of Arg310 inhibit infection- or LPS-induced pyroptosis |
774702 |
| 3.4.22.64 | proteolytic modification |
caspase-11, the murine counterpart of caspase-4, acquires protease activity within the noncanonical inflammasome by forming a dimer that self-cleaves at D285 to cleave GSDMD |
773838 |
| 3.4.22.64 | proteolytic modification |
caspases are expressed in most cells as inactive monomeric zymogens (pro-caspases), requiring processing and heterodimerization to facilitate their activation. Caspase-11 auto-proteolysis is essential for its activation and the subsequent regulation of downstream events. Caspase-11 activation, induced experimentally via its overexpression or cytoplasmic LPS stimulation, induces two autoproteolysis events, resulting in the removal of the N-terminal CARD domain from the large subunit and separating the large and small catalytic domains |
772221 |
| 3.4.22.64 | proteolytic modification |
LPS activates pro-caspase-11 cleavage and activation of caspase-11 functions |
771444 |
| 3.4.22.64 | proteolytic modification |
procaspase-11 can autoprocess itself in vitro |
647710 |
| 3.4.22.64 | proteolytic modification |
tetrameric aggregation of caspase-11 is thought to promote the autoprocessing and activation of caspase-11, activation mechanism of caspase-11, overview. The tetramerization of the N-terminal CARD prevents catalytic domain autoinhibition, leading to the caspase-11 activation. The hydrophobic interface is critical for the cellular activation of the caspase-11 inflammasome |
770172 |
| 3.4.22.64 | proteolytic modification |
the adaptor protein TRIF upregulates procaspase-11 expression, and this upregulation is required for caspase-11 processing and activation |
731611 |
| 3.4.22.64 | proteolytic modification |
the enzyme is produced as procaspase-11 and activated by proteolytic cleavage. After transcription and translation, a large amount of procaspase-11 and proIL-1beta, proIL-18 is generated and distributed in the cytoplasm. LPS binds with procaspase-11, initiate procaspase-11 oligomerization and form mature/activated caspase-11 |
770138 |
| 3.4.22.64 | 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 |
770759 |
