CASP4 forms dimers on the bacterial surface

Stable Identifier
R-HSA-9947940
Type
Reaction [binding]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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CASP4 forms dimers on the bacterial surface
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Upon sensing cytoplasmic LPS, caspase-4 (CASP4) forms oligomers/dimers (Shi J et al. 2014; Fernández-Duran I et al., 2021). Oligomerization is thought to bring CASP4 molecules into close proximity, facilitating CASP4 activation through self-cleavage (Shi J et al. 2014). SERPINB1 binding to CASP4 monomers limits the activity of CASP4 by preventing CASP4 oligomerization and activation (Choi YJ et al., 2019).
Literature References
PubMed ID Title Journal Year
25119034 Inflammatory caspases are innate immune receptors for intracellular LPS

Shi, J, Zhao, Y, Wang, Y, Gao, W, Ding, J, Li, P, Hu, L, Shao, F

Nature 2014
Participants
Input
Output
Participates
as an event of
This event is regulated
Negatively by
Regulator
CASP4:SERPINB1 [cytosol] (Homo sapiens)
Active Unit
SERPINB1 [cytosol]
Orthologous Events
CASP4 forms dimers on the bacterial surface (Bos taurus)
CASP4 forms dimers on the bacterial surface (Danio rerio)
CASP4 forms dimers on the bacterial surface (Sus scrofa)
Authored
Shamovsky, V  (2025-05-14)
Reviewed
Shi, X  (2025-08-12)
Created
Shamovsky, V  (2025-05-14)
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