OPA1 and PARL keep a lid on apoptosis.
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.
Gottlieb
Eyal
E
Apoptosis and tumour physiology laboratory, Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, Scotland G61 1BD, UK. e.gottlieb@beatson.gla.ac.uk
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000378:metabolism; D045304:Cytochromes c / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D006801:Humans; D045726:Metalloproteases / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism* / Q000648:ultrastructure; D051336:Mitochondrial Membranes / Q000378:metabolism* / Q000648:ultrastructure; D024101:Mitochondrial Proteins / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
D024101:Mitochondrial Proteins; D045304:Cytochromes c; D045726:Metalloproteases; C485223:PARL protein, human; D020169:Caspases; D020558:GTP Phosphohydrolases; C415198:OPA1 protein, human