The role of cytochrome c in caspase activation in Drosophila melanogaster cells

The role of cytochrome c in caspase activation in Drosophila melanogaster cells The release of cytochrome c from mitochondria is necessary for the formation of the Apaf-1 apoptosome and subsequent activation of caspase-9 in mammalian cells. However, the role of cytochrome c in caspase activation in Drosophila cells is not well understood. We demonstrate here that cytochrome c remains associated with mitochondria during apoptosis of Drosophila cells and that the initiator caspase DRONC and effector caspase DRICE are activated after various death stimuli without any significant release of cytochrome c in the cytosol. Ectopic expression of the proapoptotic Bcl-2 protein, DEBCL, also fails to show any cytochrome c release from mitochondria. A significant proportion of cellular DRONC and DRICE appears to localize near mitochondria, suggesting that an apoptosome may form in the vicinity of mitochondria in the absence of cytochrome c release. In vitro, DRONC was recruited to a >700-kD complex, similar to the mammalian apoptosome in cell extracts supplemented with cytochrome c and dATP. These results suggest that caspase activation in insects follows a more primitive mechanism that may be the precursor to the caspase activation pathways in mammals. DRONC; caspase activation; DRICE; apoptosis; apoptosome Footnotes ↵ * Abbreviations used in this paper: BG2, ML-DmBG2c2; GST, glutathione- S -transferase; HA, hemagglutinin; RNAi, RNA-mediated interference; RT, room temperature. Submitted: 29 November 2001 Accepted: 4 February 2002 Revision received 1 February 2002 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

The role of cytochrome c in caspase activation in Drosophila melanogaster cells

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Publisher
Rockefeller University Press
Copyright
© 2002 Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
D.O.I.
10.1083/jcb.200111107
Publisher site
See Article on Publisher Site

Abstract

The release of cytochrome c from mitochondria is necessary for the formation of the Apaf-1 apoptosome and subsequent activation of caspase-9 in mammalian cells. However, the role of cytochrome c in caspase activation in Drosophila cells is not well understood. We demonstrate here that cytochrome c remains associated with mitochondria during apoptosis of Drosophila cells and that the initiator caspase DRONC and effector caspase DRICE are activated after various death stimuli without any significant release of cytochrome c in the cytosol. Ectopic expression of the proapoptotic Bcl-2 protein, DEBCL, also fails to show any cytochrome c release from mitochondria. A significant proportion of cellular DRONC and DRICE appears to localize near mitochondria, suggesting that an apoptosome may form in the vicinity of mitochondria in the absence of cytochrome c release. In vitro, DRONC was recruited to a >700-kD complex, similar to the mammalian apoptosome in cell extracts supplemented with cytochrome c and dATP. These results suggest that caspase activation in insects follows a more primitive mechanism that may be the precursor to the caspase activation pathways in mammals. DRONC; caspase activation; DRICE; apoptosis; apoptosome Footnotes ↵ * Abbreviations used in this paper: BG2, ML-DmBG2c2; GST, glutathione- S -transferase; HA, hemagglutinin; RNAi, RNA-mediated interference; RT, room temperature. Submitted: 29 November 2001 Accepted: 4 February 2002 Revision received 1 February 2002

Journal

The Journal of Cell BiologyRockefeller University Press

Published: Mar 18, 2002

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