Liver Physiol. Of note, this domain seems to be conserved throughout evolution since it is found in numerous Bcl-2 homologs from distantly-related metazoan species (Quinn et al., 2003; Tan et al., 2007). Moreover, deletion of the C-terminal hydrophobic tail both prevented GFP-Bax redistribution and suppressed its death-promoting activity, confirming the importance of the TM domain. Pathol. Biol. doi: 10.1093/ajcp/106.5.652, Nakai, M., Takeda, A., Cleary, M. L., and Endo, T. (1993). Semin Diagn Pathol 11:223–235, Gee JMW, Robertson JFR, Ellis IO, Willsher P, McClelland RA, Hoyle HB, Kyme SR, Finlay P, Blarney RW, Nicholson RI (1994) Immunocytochemical localization of bel-2 protein in human breast cancers and its relationship to a series of prognostic markers and response to endocrine therapy. The editor and reviewers' affiliations are the latest provided on their Loop research profiles and may not reflect their situation at the time of review. This is a preview of subscription content, log in to check access. Science 226, 1097–1099. In this respect it has recently been shown that, with the notable exception of Bad, all canonical BH3-only proteins possess a functional C-terminus TM domain (Wilfling et al., 2012; Andreu-Fernández et al., 2016). In addition, the BH3-only proteins control this process by direct activation of Bax and Bak or by repressing the anti-apoptotic Bcl-2 family members (Youle and Strasser, 2008). Thus, it is tempting to speculate that Bcl-2 proteins trafficking may occur through vesicular transport inside the cell. Thus, it would be of interest to further analyse the molecular mechanisms behind Bcl-2 intracellular distribution in tumor cells (Choi et al., 2016). Cell Dev. |, Subcellular Action Range of the Bcl-2 Family of Proteins, Docking of the Bcl-2 Family of Proteins to Intracellular Membranes, Mitochondria-to-Cytosol Bax and Bak Trafficking, Bax and Bak Trafficking through Peroxisome/Lysosome Pathways, Moonlighting Functions of the Bcl-2 Proteins in Respect to their Subcellular Localizations, Creative Commons Attribution License (CC BY). (2001). 53, 4701–4714. (2012). (2017). doi: 10.1083/jcb.200210084, Kim, H., Tu, H. C., Ren, D., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., et al. (2008). J. Biol. U.S.A. 113, E1953–E1962. Although being predominantly mitochondrial, Bak leads to apoptosis only in the presence of apoptotic stimuli (Todt et al., 2015). Cell Death Differ. For instance, the human FK506-binding protein 38 (FKBP38), a mitochondrial chaperone, is able to interact with and effectively target Bcl-2 to the mitochondria (Shirane and Nakayama, 2003). Intracellular vesicles—along with protein-protein interactions—could be responsible for the transit of Bcl-2 proteins inside the cell as suggested in the case of peroxisomal Bak. 428, 31–35. Mod Pathol 6:660–662, Siziopikou KP, Prioleau J, Schnitt S (1996) MIB-1 proliferation index (PI) in ductal carcinoma in situ (DCIS): relationship to bcl-2 and p53 protein. doi: 10.1101/gad.1553607, Germain, M., Mathai, J. P., and Shore, G. C. (2002). Importantly, they noticed that GFP-Bax redistribution took place before apoptotic cells shrinkage. Nat. Cell Dev. J. Biol. In this regard, peroxisomes play an important role in ER-mitochondria protein exchanges. Oberle, C., Huai, J., Reinheckel, T., Tacke, M., Rassner, M., Ekert, P. G., et al. Finally, Bcl-2 proteins are major trans-regulating elements that control Bax subcellular localization. Nat. 288, 25340–25349. Subcellular localization of the bcl-2 protein in malignant and normal lymphoid cells.

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