OPA1 and PARL keep a lid on apoptosis

Cell. 2006 Jul 14;126(1):27-9. doi: 10.1016/j.cell.2006.06.030.

Abstract

A change in the shape of mitochondrial cristae must take place to attain rapid and complete release of cytochrome c during apoptosis. In this issue of Cell, Cipolat et al. and Frezza et al. (2006) show that a rhomboid intramembrane protease PARL and a dynamin-related protein OPA1 are critical regulators of cristae remodeling.

Publication types

  • Comment
  • Review

MeSH terms

  • Animals
  • Apoptosis / physiology*
  • Caspases / metabolism
  • Cytochromes c / metabolism
  • GTP Phosphohydrolases / metabolism*
  • Humans
  • Metalloproteases / metabolism*
  • Mitochondria / metabolism*
  • Mitochondria / ultrastructure
  • Mitochondrial Membranes / metabolism*
  • Mitochondrial Membranes / ultrastructure
  • Mitochondrial Proteins / metabolism*
  • Signal Transduction / physiology

Substances

  • Mitochondrial Proteins
  • Cytochromes c
  • Metalloproteases
  • PARL protein, human
  • Caspases
  • GTP Phosphohydrolases
  • OPA1 protein, human