Caspase-mediated cleavage of TJP1

Stable Identifier
R-HSA-351913
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Cleavage of the C-terminal cytoplasmic domain of occludin during apoptosis generates a fragment that can no longer associate with the cytoplasmic adapter proteins ZO-1, -2 and -3 and, as a consequence, with the actin cytoskeleton (Bojarski et al., 2003). Cleavage of ZO-1 and ZO-2 further disrupts tight junction structure and function. Notably, claudins, which are associated with ZO-1, ZO-2 and ZO-3, completely lose their linkage to the actin cytoskeleton and other ZO-1-, ZO-2-, ZO-3-interacting proteins (Bojarski et al., 2003). Caspase-3 was found to be responsible for TJP1 (ZO-1) cleavage in both dog and mouse cells (Chin et al. 2006, Zehendner et al. 2011).
Literature References
PubMed ID Title Journal Year
15054114 The specific fates of tight junction proteins in apoptotic epithelial cells

Fromm, M, Mankertz, J, Weiske, J, Florian, P, Tauber, R, Schulzke, JD, Schröder, W, Bojarski, C, Huber, O, Schöneberg, T

J Cell Sci 2004
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Catalyst Activity

cysteine-type endopeptidase activity of Caspase-3 [cytosol]

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