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Colin, J., Garibal, J., Clavier, A., Rincheval-Arnold, A., Gaumer, S., Mignotte, B., Guénal, I. (2014). The drosophila Bcl-2 family protein Debcl is targeted to the proteasome by the β-TrCP homologue slimb.  Apoptosis 19(10): 1444--1456.
FlyBase ID
FBrf0226227
Publication Type
Research paper
Abstract
The ubiquitin-proteasome system is one of the main proteolytic pathways. It inhibits apoptosis by degrading pro-apoptotic regulators, such as caspases or the tumor suppressor p53. However, it also stimulates cell death by degrading pro-survival regulators, including IAPs. In Drosophila, the control of apoptosis by Bcl-2 family members is poorly documented. Using a genetic modifier screen designed to identify regulators of mammalian bax-induced apoptosis in Drosophila, we identified the ubiquitin activating enzyme Uba1 as a suppressor of bax-induced cell death. We then demonstrated that Uba1 also regulates apoptosis induced by Debcl, the only counterpart of Bax in Drosophila. Furthermore, we show that these apoptotic processes involve the same multimeric E3 ligase-an SCF complex consisting of three common subunits and a substrate-recognition variable subunit identified in these processes as the Slimb F-box protein. Thus, Drosophila Slimb, the homologue of β-TrCP targets Bax and Debcl to the proteasome. These new results shed light on a new aspect of the regulation of apoptosis in fruitfly that identifies the first regulation of a Drosophila member of the Bcl-2 family.
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Apoptosis
    Title
    Apoptosis. An international journal on programmed cell death.
    Publication Year
    1996-
    ISBN/ISSN
    1360-8185
    Data From Reference
    Alleles (17)
    Genes (10)
    Physical Interactions (2)
    Natural transposons (1)
    Insertions (1)
    Experimental Tools (3)
    Transgenic Constructs (8)