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Background
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CASP6 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein could be processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade.
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Background
References
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- Schmeck, B., et al., Infect. Immun. 72(9):4940-4947 (2004).
- Mendez, E., et al., J. Virol. 78(16):8601-8608 (2004).
- MacLachlan, T.K., et al., Proc. Natl. Acad. Sci. U.S.A. 99(14):9492-9497 (2002).
- Sordet, O., et al., Leukemia 16(8):1569-1570 (2002).
- LeBlanc, A., et al., J. Biol. Chem. 274(33):23426-23436 (1999).
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