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Type: Journal article
Title: The two cytochrome c species, DC3 and DC4, are not required for caspase activation and apoptosis in Drosophila cells
Author: Dorstyn, L.
Mills, K.
Lazebnik, Y.
Kumar, S.
Citation: Journal of Cell Biology, 2004; 167(3):405-410
Publisher: Rockefeller Univ Press
Issue Date: 2004
ISSN: 0021-9525
Statement of
Loretta Dorstyn, Kathryn Mills, Yuri Lazebnik, and Sharad Kumar
Abstract: In Drosophila, activation of the apical caspase DRONC requires the apoptotic protease-activating factor homologue, DARK. However, unlike caspase activation in mammals, DRONC activation is not accompanied by the release of cytochrome c from mitochondria. Drosophila encodes two cytochrome c proteins, Cytc-p (DC4) the predominantly expressed species, and Cytc-d (DC3), which is implicated in caspase activation during spermatogenesis. Here, we report that silencing expression of either or both DC3 and DC4 had no effect on apoptosis or activation of DRONC and DRICE in Drosophila cells. We find that loss of function mutations in dc3 and dc4, do not affect caspase activation during Drosophila development and that ectopic expression of DC3 or DC4 in Drosophila cells does not induce caspase activation. In cell-free studies, recombinant DC3 or DC4 failed to activate caspases in Drosophila cell lysates, but remarkably induced caspase activation in extracts from human cells. Overall, our results argue that DARK-mediated DRONC activation occurs independently of cytochrome c.
Keywords: Cell Line; Animals; Humans; Drosophila melanogaster; Cytochrome c Group; Cytochromes c; Caspases; Drosophila Proteins; Recombinant Proteins; Apoptosis; Enzyme Activation; Protein Binding; Mutation
RMID: 0020041011
DOI: 10.1083/jcb.200408054
Appears in Collections:Medicine publications

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