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Many cuts to ruin: a comprehensive update of caspase substrates

Open access
Fischer, U, Jänicke, R U, Schulze-Osthoff, K·2003·Cell Death & Differentiation

Abstract

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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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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CoChat. (2026). Citation check: Many cuts to ruin: a comprehensive update of caspase substrates. https://app.cochat.ai/papers/10.1038/sj.cdd.4401160
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Fischer, U., Jänicke, R. U., & Schulze-Osthoff, K. (2003). Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death & Differentiation. https://doi.org/10.1038/sj.cdd.4401160

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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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