Study Bax and Debcl pro-apoptotic activities
 

Proteins of the Bcl-2 (B Cell Lymphoma 2) family are among the main effectors of cell death by apoptosis (review: (Estaquier et al., 2012)). Two genes of the bcl-2 family are present in Drosophila (buffy and debcl) (review: (Clavier et al., 2016a)). We have shown that, in Drosophila, Bax induces an executionner caspase-independent cell death process involving mitochondrial events (Gaumer et al., 2000 ; Brun et al., 2002 ; Colin et al., 2009b).

More recently, we isolated several suppressors of bax. This screen allowed us to show that glycerophosphate oxidase-1 participates in debcl-induced apoptosis by increasing mitochondrial reactive oxygen species production (Colin et al. 2015). The study of these suppressors also allowed us to highlight a regulation of Bax and Debcl-induced apoptosis by the proteasome and to show that Debcl is targeted to the proteasome by the E3 ligase Slimb, the ß-TrCP homolog (Colin et al. 2014).

As part of our study of RBF-induced apoptosis, we also showed that Debcl and the fission protein Drp1 can interact and that Buffy inhibits this interaction (Clavier et al., 2015). Moreover, apoptosis induced by Debcl requires Drp1 and involves mitochondrial fragmentation. These results provide a mechanism by which Debcl can control apoptosis and shed light on a link between Bcl-2 family members and mitochondrial dynamics during cell death in vivo.
 

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