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

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

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.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis*
  • Caspases / metabolism*
  • Enzyme Activation
  • Humans
  • Phosphorylation
  • Protein Processing, Post-Translational*
  • Ubiquitination

Substances

  • Caspases