Abstract
Bcl-2 family proteins play a central role in regulating apoptosis. We previously reported that human Bcl-rambo, also termed BCL2L13, localized to mitochondria and induced apoptosis when overexpressed in human embryonic kidney 293T cells. However, the physiological function of Bcl-rambo currently remains unclear. In the present study, human Bcl-rambo was ectopically expressed in Drosophila melanogaster. Bcl-rambo mainly localized to the mitochondria of Drosophila Schneider 2 (S2) cells. The overexpression of Bcl-rambo, but not Bcl-rambo lacking a C-terminal transmembrane domain, induced apoptosis in S2 cells. Moreover, the ectopic expression of Bcl-rambo by a GAL4-UAS system induced aberrant morphological changes characterized by atrophied wing, split thorax, and rough eye phenotypes. Bcl-rambo induced the activation of effector caspases in eye imaginal discs. The rough eye phenotype induced by Bcl-rambo was partly rescued by the co-expression of p35, Diap1, and Diap2. By using this Drosophila model, we showed that human Bcl-rambo interacted genetically with Drosophila homologues of adenine nucleotide translocators and the autophagy-related 8 protein. The results of the present study demonstrated that human Bcl-rambo localized to mitochondria and at least regulated an apoptosis signaling pathway in Drosophila.
Highlights
Programmed cell death plays an essential role in the development and maintenance of tissue homeostasis in animals [1]
We previously identified the widely expressed Bcl-2 family protein Bcl-rambo, termed BCL2L13 (Fig 1A) [12], and showed that it was composed of four N-terminal Bcl-2 homology (BH) domains (i.e., BH1, BH2, BH3, and BH4), a unique 250 amino acid extension termed the BHNo domain, and a C-terminal transmembrane domain (TM) [12]
We demonstrated that the ectopic expression of Bcl-rambo in transgenic flies induced apoptosis and caused aberrant morphological changes, including a rough eye phenotype
Summary
Programmed cell death plays an essential role in the development and maintenance of tissue homeostasis in animals [1]. Apoptosis is one type of programmed cell death that is mainly regulated by a family of cysteinyl aspartate-specific proteinases (caspases) [2]. Caspases have been classified as initiator caspases (e.g., caspase-8, -9, and -10) and effector caspases
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