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Trends Cell Biol. 2017 May;27(5):322-339. doi: 10.1016/j.tcb.2017.01.003. Epub 2017 Feb 7.

Post-translational Modification of Caspases: The Other Side of Apoptosis Regulation.

Author information

1
Faculty of Basic Medicine, MV Lomonosov Moscow State University, 119991 Moscow, Russia.
2
Faculty of Basic Medicine, MV Lomonosov Moscow State University, 119991 Moscow, Russia; Division of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, Box 210, 17177 Stockholm, Sweden. Electronic address: boris.zhivotovsky@ki.se.
3
Faculty of Basic Medicine, MV Lomonosov Moscow State University, 119991 Moscow, Russia; Department of Translational Inflammation, Institute of Experimental Internal Medicine, Otto von Guericke University, Magdeburg, Germany. Electronic address: inna.lavrik@med.ovgu.de.

Abstract

Apoptosis is a crucial program of cell death that controls development and homeostasis of multicellular organisms. The main initiators and executors of this process are the Cysteine-dependent ASPartate proteASES - caspases. A number of regulatory circuits tightly control caspase processing and activity. One of the most important, yet, at the same time still poorly understood control mechanisms of activation of caspases involves their post-translational modifications. The addition and/or removal of chemical groups drastically alters the catalytic activity of caspases or stimulates their nonapoptotic functions. In this review, we will describe and discuss the roles of key caspase modifications such as phosphorylation, ubiquitination, nitrosylation, glutathionylation, SUMOylation, and acetylation in the regulation of apoptotic cell death and cell survival.

KEYWORDS:

apoptosis; caspases; post-translational modifications

PMID:
28188028
DOI:
10.1016/j.tcb.2017.01.003
[Indexed for MEDLINE]

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