Many cuts to ruin: a comprehensive update of caspase substrates

By U. Fischer, R. Jänicke, K. Schulze-Osthoff. Cell Death and Differentiation, 2003

1,130 citations recorded by the source corpus.

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.

Subfields: Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/bda18c150a0104cdc49e34a35e9cea4972fb8b19

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Citations in the corpus

PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration (2010, background): “Caspase mediated apoptotic cell death is accomplished through the cleavage of several key proteins required for cellular functioning and survival [62].”
Hydrogen peroxide induces apoptotic-like cell death in Microcystis aeruginosa (Chroococcales, Cyanobacteria) in a dose-dependent manner (2012, background): “Within the caspase family, caspase- 3 is believed to be the final executor of apoptotic cell death; it elicits organized degradation of many cellular proteins, and it changes the nuclear morphology (Fischer et al. 2003; Rice & Bayles 2008).”
Caspases in cell survival, proliferation and differentiation (2007, background): “The cleavage of several adhesion- and cell motility-related proteins during mammalian apoptosis may also point to a role in the regulation of cell migration.(86) Recent findings are in support of this suggestion as cell migration is severely hampered in caspase-8-deficient cells and CrmA-overexpress”
Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family (2006, background): “Using a mechanism reminiscent of classical protease activation, the executioner caspase zymogens are cleaved in their interchain linker and, once active, are responsible for most of the proteolytic events that destroy the cell (Fischer et al, 2003).”