Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1

Oncogene. 2010 Mar 25;29(12):1717-9. doi: 10.1038/onc.2009.519. Epub 2010 Jan 25.

Abstract

Beclin 1 has a key role in the initiation of autophagy, a process of self-cannibalism in which cytoplasmic constituents are sequestered and targeted for lysosomal degradation. In a recent issue of Cell Death & Disease, Wirawan et al. report the significant finding that caspases can cleave Beclin 1, thereby destroying its pro-autophagic activity. Moreover, the C-terminal fragment of Beclin 1 that results from this cleavage acquires a new function and can amplify mitochondrion-mediated apoptosis. Of note, the BH3 domain of Beclin 1 remains within the N-terminal fragment, which has no detectable pro-apoptotic activity. These findings provide important insights into the molecular cross talk between autophagy and apoptosis.

Publication types

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

MeSH terms

  • Apoptosis / physiology*
  • Apoptosis Regulatory Proteins / metabolism*
  • Autophagy / physiology*
  • Beclin-1
  • Caspases / metabolism*
  • Cell Death / physiology
  • Cell Physiological Phenomena / physiology
  • Homeostasis
  • Humans
  • Intracellular Membranes / physiology
  • Lysosomes / physiology
  • Membrane Proteins / metabolism*
  • Mitochondria / physiology
  • Models, Biological

Substances

  • Apoptosis Regulatory Proteins
  • BECN1 protein, human
  • Beclin-1
  • Membrane Proteins
  • Caspases