Caspase-mediated cleavage of Z0-2

Stable Identifier
Reaction [transition]
Homo sapiens
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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). Inhibition of caspase-3 prevents cleavage of ZO-2, implicating caspase-3 as the responsible endopeptidase (Bojarski et al. 2004).

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
Catalyst Activity

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

Orthologous Events
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