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Many cuts to ruin: a comprehensive update of caspase substrates
Open accessAbstract
AbstractApoptotic cell death is executed by the caspase-mediated cleavage of various vital proteins. Elucidating the consequences of this endoproteolytic cleavage is crucial for our understanding of cell death and other biological processes. Many caspase substrates are just cleaved as bystanders, because they happen to contain a caspase cleavage site in their sequence. Several targets, however, have a discrete function in propagation of the cell death process. Many structural and regulatory proteins are inactivated by caspases, while other substrates can be activated. In most cases, the consequences of this gain-of-function are poorly understood. Caspase substrates can regulate the key morphological changes in apoptosis. Several caspase substrates also act as transducers and amplifiers that determine the apoptotic threshold and cell fate. This review summarizes the known caspase substrates comprising a bewildering list of more than 280 different proteins. We highlight some recent aspects inferred by the cleavage of certain proteins in apoptosis. We also discuss emerging themes of caspase cleavage in other forms of cell death and, in particular, in apparently unrelated processes, such as cell cycle regulation and cellular differentiation.
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Cites
Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing
Sebbagh, M., Renvoizé, C., Hamelin, J., Riché, N., Bertoglio, J., & Bréard, J. (2001) · Nature Cell Biology · doi:10.1038/35070019 · Cited by 915
Functional consequences of caspase activation in cardiac myocytes
Communal, C., Sumandea, M., de Tombe, P., Narula, J., Solaro, R. J., & Hajjar, R. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092022999 · Cited by 390
Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis
Canu, N., Dus, L., Barbato, C., Ciotti, M. T., Brancolini, C., Rinaldi, A. M., Novak, M., Cattaneo, A., Bradbury, A., & Calissano, P. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-18-07061.1998 · Cited by 232
Marissen, W. E., & Lloyd, R. E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7565 · Cited by 198
Proteolytic Cleavage of the mdm2 Oncoprotein during Apoptosis
Chen, L., Marechal, V., Moreau, J., Levine, A. J., & Chen, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22966 · Cited by 121
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Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family
Eckelman, B. P., Salvesen, G. S., & Scott, F. L. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400795 · Cited by 813
Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Franklin, C. C., Backos, D. S., Mohar, I., White, C. C., Forman, H. J., & Kavanagh, T. J. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.009 · Cited by 438
Cell death in planktonic, photosynthetic microorganisms
Bidle, K. D., & Falkowski, P. G. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro956 · Cited by 344
Antiproliferation and induction of apoptosis by Moringa oleifera leaf extract on human cancer cells
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Metadata
- Authors
- Fischer, U., Jänicke, R. U., & Schulze-Osthoff, K.
- Venue
- Cell Death & Differentiation
- Published
- 2003-01
- Volume
- 10
- Issue
- 1
- Pages
- 76-100
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- OpenAlex
- W2142911981
- Cited by
- 1,029
- References
- 5
- FWCI
- 29.38
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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