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BCL-2 family proteins: changing partners in the dance towards death
Open accessAbstract
The BCL-2 family of proteins controls cell death primarily by direct binding interactions that regulate mitochondrial outer membrane permeabilization (MOMP) leading to the irreversible release of intermembrane space proteins, subsequent caspase activation and apoptosis. The affinities and relative abundance of the BCL-2 family proteins dictate the predominate interactions between anti-apoptotic and pro-apoptotic BCL-2 family proteins that regulate MOMP. We highlight the core mechanisms of BCL-2 family regulation of MOMP with an emphasis on how the interactions between the BCL-2 family proteins govern cell fate. We address the critical importance of both the concentration and affinities of BCL-2 family proteins and show how differences in either can greatly change the outcome. Further, we explain the importance of using full-length BCL-2 family proteins (versus truncated versions or peptides) to parse out the core mechanisms of MOMP regulation by the BCL-2 family. Finally, we discuss how post-translational modifications and differing intracellular localizations alter the mechanisms of apoptosis regulation by BCL-2 family proteins. Successful therapeutic intervention of MOMP regulation in human disease requires an understanding of the factors that mediate the major binding interactions between BCL-2 family proteins in cells.
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“Bcl-2 family plays a crucial role in the endogenous apoptosis signal transduction pathway by regulating the mitochondrial/cytochrome C-mediated apoptosis process.356,357”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [357]
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ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets
Souers, A. J., Leverson, J. D., Boghaert, E. R., Ackler, S. L., Catron, N. D., Chen, J., Dayton, B. D., Ding, H., Enschede, S. H., Fairbrother, W. J., et al. (2013) · Nature Medicine · doi:10.1038/nm.3048 · Cited by 3,058
Caspase Functions in Cell Death and DiseasePreprint
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,702
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
ABT-263: A Potent and Orally Bioavailable Bcl-2 Family Inhibitor
Tse, C., Shoemaker, A. R., Adickes, J., Anderson, M. G., Chen, J., Jin, S., Johnson, E. F., Marsh, K. C., Mitten, M. J., Nimmer, P., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5836 · Cited by 1,992
Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., & Huang, D. C. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.030 · Cited by 1,816
Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane
Kuwana, T., Mackey, M. R., Perkins, G. A., Ellisman, M. H., Latterich, M., Schneiter, R., Green, D. R., & Newmeyer, D. D. (2002) · Cell · doi:10.1016/s0092-8674(02)01036-x · Cited by 1,513
Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis
Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H. S., Shuker, S. B., Chang, B. S., Minn, A. J., et al. (1997) · Science · doi:10.1126/science.275.5302.983 · Cited by 1,476
BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387
Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix
Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349
Certo, M. V., Moore, V. D. G., Nishino, M., Wei, G., Korsmeyer, S. J., Armstrong, S. A., & Letai, A. G. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.027 · Cited by 1,278
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Chen, J., Li, G., He, X., Chen, Z., Chen, Z., Liu, D., Guo, S., Huang, T., Lan, P., Lan, P., et al. (2023) · Gastroenterology report · doi:10.1093/gastro/goae045 · Cited by 16
Guo, X., He, L., Xu, W., Wang, W., Feng, X., Fu, Y., Zhang, X., Ding, R., Qi, X., Bao, J., et al. (2024) · Marine Drugs · doi:10.3390/md22060252 · Cited by 15
Winter, R., Amghar, M., Wacker, A. S., Bakos, G., Taş, H., Roscher, M., Kelly, J. M., & Benešová, M. (2024) · Pharmaceuticals · doi:10.3390/ph17081031 · Cited by 16
Rak-Pasikowska, A., Hałucha, K., Kamińska, M., Niewiadomska, J., Noszczyk-Nowak, A., & Bil‐Lula, I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212253 · Cited by 15
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Lamsira, H. K., Sabatini, A., Ciolfi, S., Ciccosanti, F., Sacchi, A., Piacentini, M., & Nardacci, R. (2025) · Cells · doi:10.3390/cells14050351 · Cited by 17
Asemani, Y., Azadmehr, A., Hajiaghaee, R., & Amirghofran, Z. (2018) · DARU Journal of Pharmaceutical Sciences · doi:10.1007/s40199-018-0219-z · Cited by 15
Effect of IL‑7 on Th17 cell responses in a mouse model of neutrophilic asthma
Zhang, X., Zhang, M., Jiang, M., & Nong, G. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11191 · Cited by 15
Suppressor of Ty 16 promotes lung cancer malignancy and is negatively regulated by miR‐1227‐5p
Yang, L., Wang, X., Jiao, X., Tian, B., Zhang, M., Zhou, C., Wang, R., Chen, H., Wang, B., Li, J., et al. (2020) · Cancer Science · doi:10.1111/cas.14627 · Cited by 15
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Ren, Y., Huang, S.-H., Macedo, A. B., Ward, A. R., Alberto, W. D. C., Klevorn, T., Leyre, L., Copertino, D. C., Mota, T. M., Chan, D., et al. (2021) · Journal of Virology · doi:10.1128/jvi.02425-20 · Cited by 15
Yu, W. S., Kwon, S., Agadagba, S. K., Chan, L.-L.-H., Wong, K.-H., & Lim, L. W. (2021) · Cells · doi:10.3390/cells10092492 · Cited by 16
Nuamnaichati, N., Parichatikanond, W., & Mangmool, S. (2021) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001159 · Cited by 15
Dashti, A., Shokrzadeh, M., Karami, M. Y., & Habibi, E. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e08940 · Cited by 15
Lachowiez, C. A., Atluri, H., & Dinardo, C. D. (2022) · Therapeutic Advances in Hematology · doi:10.1177/20406207221093964 · Cited by 15
Vilková, M., Michalková, R., Kello, M., Sabolová, D., Takáč, P., Kudlicková, Z., Garberová, M., Tvrdoňová, M., Béreš, T., & Mojžíš, J. (2022) · Medicinal Chemistry Research · doi:10.1007/s00044-022-02911-0 · Cited by 15
Singh, M., Gupta, R., Comez, L., Paciaroni, A., Rani, R., & Kumar, V. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.06.002 · Cited by 13
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Kim, S., Park, H.-S., & Oh, B. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.06.021 · Cited by 15
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Lucas, S. C. C., Milbradt, A. G., Blackwell, J. H., Bonomo, S., Brierley, A., Cassar, D. J., Freeman, J., Hadfield, T. E., Morrill, L. A., Riemens, R., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00781 · Cited by 15
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Li, Z., Du, X., Yang, Y., Li, Z., Chen, P., Kan, Y., Pan, J., Lin, L., Liu, D. X., Jiang, X., et al. (2024) · Brain · doi:10.1093/brain/awae304 · Cited by 14
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Loncke, J., de Ridder, I., Kale, J., Wagner, L. E., Kaasik, A., Parys, J. B., Kerkhofs, M., Andrews, D. W., Yule, D. I., Vervliet, T., et al. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119857 · Cited by 14
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Qi, Q., Xue, Y., Lv, J., Sun, D., Du, J., Cai, S., Li, Y., Gu, T., & Wang, M. (2018) · Oncology Letters · doi:10.3892/ol.2018.8177 · Cited by 14
Derf, A., Mudududdla, R., Akintade, D. D., Williams, I. S., Abdullaha, M., Chaudhuri, B., & Bharate, S. B. (2018) · ACS Omega · doi:10.1021/acsomega.8b01154 · Cited by 14
Svobodová, J., Procházková, J., Kabátková, M., Krkoška, M., Šmerdová, L., Líbalová, H., Topinka, J., Kléma, J., Kozubı́k, A., Machala, M., et al. (2019) · Toxicological Sciences · doi:10.1093/toxsci/kfz202 · Cited by 14
Häusler, E., Fredriksson, K., Goba, I., Peters, C., Raltchev, K., Sperl, L. E., Steiner, A., Weinkauf, S., & Hagn, F. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183190 · Cited by 14
Anaya‐Eugenio, G. D., Carcache, P. J. B., Ninh, T. N., Ren, Y., Soejarto, D. D., & Kinghorn, A. D. (2020) · Phytotherapy Research · doi:10.1002/ptr.6930 · Cited by 14
Vishnu, W. K., Abeesh, P., & Guruvayoorappan, C. (2021) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2021.115491 · Cited by 14
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Krivokolysko, D. S., Dotsenko, V. V., Bibik, E. Y., Miazina, A. V., Krivokolysko, S. G., Vasilin, V. K., Pankov, A. A., Aksenov, N. A., & Aksenova, I. V. (2021) · Russian Journal of General Chemistry · doi:10.1134/s1070363221120306 · Cited by 14
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Jin, Y., Zhou, Q., Geng, J., Meng, Q., Wei, Z., Ding, M., Zhou, J., Zeng, Y., Cao, W., Liu, F., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.792360 · Cited by 14
Huang, Y., Meng, X., Zhou, Z. Y., Zhu, W., Chen, X., He, Y., He, N., Han, X., Zhou, D., Duan, X., et al. (2022) · Journal of Materials Chemistry B · doi:10.1039/d2tb01247b · Cited by 14
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Johnson, L. A., Rodansky, E. S., Tran, A., Collins, S., Eaton, K. A., Malamet, B. J., Steiner, C. A., Huang, S., Spence, J. R., & Higgins, P. (2021) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izab166 · Cited by 13
Hsieh, M., Hsieh, M., Lo, Y., Lin, C., Chuang, Y., Chen, M., & Chou, M. (2022) · Environmental Toxicology · doi:10.1002/tox.23502 · Cited by 13
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Barillé‐Nion, S., Lohard, S., & Juin, P. P. (2020) · Biomolecules · doi:10.3390/biom10081109 · Cited by 16
Klimentova, E. A., Suchkov, I. A., Egorov, A. A., & Kalinin, R. E. (2020) · Современные технологии в медицине · doi:10.17691/stm2020.12.4.13 · Cited by 34
Huang, S., Tuergong, G., Zhu, H., Wang, X. B., Weng, G., & Yu, R. (2020) · Acta Pharmaceutica · doi:10.2478/acph-2021-0012 · Cited by 13
Drastichová, Z., Rudajev, V., Pallag, G., & Novotný, J. (2021) · Biological Research · doi:10.1186/s40659-021-00327-5 · Cited by 12
Tian, M., Cao, H., Gao, H., Zhu, L., Wu, Y., & Li, G. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116972 · Cited by 12
Rhamnetin ameliorates non-alcoholic steatosis and hepatocellular carcinoma in vitro
Shatta, M. A., El-Derany, M. O., Gibriel, A. A., & EL-Mesallamy, H. O. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04619-6 · Cited by 13
Liang, Y., Qian, Y., Tang, J., Yao, C., Yu, S., Qu, J., Wei, H., Chen, G., & Han, Y. K. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110304 · Cited by 13
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Scimeca, M., Rovella, V., Palumbo, V., Scioli, M. P., Bonfiglio, R., Melino, G., Piacentini, M., Frati, L., Agostini, M., Candi, E., et al. (2023) · Cancers · doi:10.3390/cancers15143638 · Cited by 14
Mazandarani, A., Taravati, A., Mohammadnejad, J., & Yazdian, F. A. (2023) · Chemistry & Biodiversity · doi:10.1002/cbdv.202300659 · Cited by 12
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Cao, L., Wu, Y.-K., Lin, T.-X., Lin, M., Chen, Y., Wang, L.-Q., Wang, J., Lin, J., Lü, J., Chen, Q., et al. (2023) · Cancer Cell International · doi:10.1186/s12935-023-03112-4 · Cited by 12
Progress of natural sesquiterpenoids in the treatment of hepatocellular carcinoma
Wang, X., Meng, F., & Mao, J. (2024) · World Journal of Hepatology · doi:10.3389/fonc.2024.1445222 · Cited by 13
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Wyżewski, Z., Gregorczyk-Zboroch, K. P., Mielcarska, M. B., Świtlik, W. Z., & Niedzielska, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062385 · Cited by 12
Age-Dependent Differential Expression of Apoptotic Markers in Rat Oral Mucosa
Elias, W. Y. (2018) · Asian Pacific Journal of Cancer Prevention · doi:10.31557/apjcp.2018.19.11.3245 · Cited by 12
Lan, W., Lin, J., Liu, W., Wang, F., & Xie, Y. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135615 · Cited by 12
Computational study on novel natural inhibitors targeting BCL2
Lv, X., Jiang, Y., Wang, X., Xie, H., Dou, G., Wang, J., Yang, W., Wang, H., Li, Z., Zhang, X., et al. (2021) · Medical Oncology · doi:10.1007/s12032-021-01513-x · Cited by 12
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Zhang, X., Xie, J., Sun, H., Wei, Q., & Nong, G. (2021) · Immunological Investigations · doi:10.1080/08820139.2021.1928183 · Cited by 12
Momeny, M., Shamsaiegahkani, S., Kashani, B., Hamzehlou, S., Esmaeili, F., Yousefi, H., Irani, S., Mousavi, S. A., & Ghaffari, S. H. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.120100 · Cited by 12
Senichkin, V. V., Pervushin, N. V., Zamaraev, A. V., Sazonova, E. V., Zuev, A. P., Streletskaia, A. Y., Prikazchikova, T. A., Zatsepin, T. S., Kovaleva, O. V., Tchevkina, E. M., et al. (2021) · Cancers · doi:10.3390/cancers14010181 · Cited by 12
Ibrahim, S., Fahim, S. A., Tadros, S. A., & Badary, O. A. (2022) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23078 · Cited by 12
Jang, W. Y., Kim, D. S., Park, S. H., Yoon, J. H., Shin, C. Y., Huang, L., Nang, K., Kry, M., Byun, H.-W., Lee, B., et al. (2022) · Molecules · doi:10.3390/molecules27134086 · Cited by 12
Metadata
- Authors
- Kale, J., Osterlund, E. J., & Andrews, D. W.
- Affiliations
- Sunnybrook Hospital (CA)
- University of Toronto (CA)
- Corresponding author
- Andrews, David W
- Venue
- Cell Death & Differentiation
- Published
- 2017-11-17
- Volume
- 25
- Issue
- 1
- Pages
- 65-80
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- PMC
- PMC5729540
- OpenAlex
- W2769631482
- Cited by
- 1,574
- References
- 120
- Citations by year
- 2026: 123 · 2025: 189 · 2024: 225 · 2023: 231 · 2022: 242 · 2021: 228 · 2020: 155 · 2019: 123 · 2018: 52 · 2017: 3
- FWCI
- 8.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell Death and Differentiation (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research ((FDN143312))
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- Bcl-2 family proteins, mitochondrial outer membrane permeabilization, apoptosis, anti-apoptotic proteins, pro-apoptotic proteins, protein-protein interaction, binding affinity, protein concentration, post-translational modification, subcellular localization, caspase activation, cell fate regulation
- MeSH terms
- Cell Membrane Permeability, Protein Processing, Post-Translational, Apoptosis, Proto-Oncogene Proteins c-bcl-2, bcl-2 Homologous Antagonist-Killer Protein, Apoptosis Regulatory Proteins, bcl-2-Associated X Protein, Mitochondrial Membranes
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