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- W2142911981 abstract "Apoptotic 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." @default.
- W2142911981 created "2016-06-24" @default.
- W2142911981 creator A5046439201 @default.
- W2142911981 creator A5055378278 @default.
- W2142911981 creator A5074047222 @default.
- W2142911981 date "2003-01-01" @default.
- W2142911981 modified "2023-10-15" @default.
- W2142911981 title "Many cuts to ruin: a comprehensive update of caspase substrates" @default.
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