Many cuts to ruin: a comprehensive update of caspase substrates
Top Cited Papers
- 1 January 2003
- journal article
- review article
- Published by Springer Nature in Cell Death & Differentiation
- Vol. 10 (1) , 76-100
- https://doi.org/10.1038/sj.cdd.4401160
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.Keywords
This publication has 345 references indexed in Scilit:
- Active Caspase-8 Translocates into the Nucleus of Apoptotic Cells to Inactivate Poly(ADP-ribose) Polymerase-2Journal of Biological Chemistry, 2002
- Caspase-mediated Cleavage of the Ca2+/Calmodulin-dependent Protein Kinase-like Kinase Facilitates Neuronal ApoptosisPublished by Elsevier ,2001
- Vitamin D3-induced Apoptosis of Murine Squamous Cell Carcinoma CellsJournal of Biological Chemistry, 2001
- Caspases mediate nucleoporin cleavage, but not early redistribution of nuclear transport factors and modulation of nuclear permeability in apoptosisCell Death & Differentiation, 2001
- c-IAP1 Is Cleaved by Caspases to Produce a Proapoptotic C-terminal FragmentJournal of Biological Chemistry, 2001
- The 72-kDa Component of Signal Recognition Particle Is Cleaved during ApoptosisPublished by Elsevier ,1998
- Caspase-3 Is Required for DNA Fragmentation and Morphological Changes Associated with ApoptosisJournal of Biological Chemistry, 1998
- The Proteolytic Cleavage of Protein Kinase C Isotypes, Which Generates Kinase and Regulatory Fragments, Correlates with Fas‐Mediated and 12‐O‐Tetradecanoyl‐Phorbol‐13‐Acetate‐Induced ApoptosisEuropean Journal of Biochemistry, 1997
- Specific Cleavage of the Large Subunit of Replication Factor C in Apoptosis Is Mediated by CPP32-like ProteaseBiochemical and Biophysical Research Communications, 1997
- A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytesNature, 1992