Reactome | Caspase-mediated cleavage of Z0-2

Caspase-mediated cleavage of Z0-2

Stable Identifier

R-HSA-351871

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane

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). 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 Bojarski, C, Weiske, J, Schöneberg, T, Schröder, W, Mankertz, J, Schulzke, JD, Florian, P, Fromm, M, Tauber, R, Huber, O	J Cell Sci	2004