Cited by 658Cell death mechanisms and regulationCancer-related Molecular PathwaysAutophagy in Disease and Therapy

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Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis

Puthalakath, Hamsa, Villunger, Andreas, O'Reilly, Lorraine A., Beaumont, Jennifer G., Coultas, Leigh, Cheney, Richard E., Huang, David C. S., Strasser, Andreas·2001·Science

DOI 10.1126/science.1062257

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Abstract

Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is required both for binding to prosurvival Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors by association with dynein light chain 2. Certain damage signals, such as loss of cell attachment (anoikis), unleash Bmf, allowing it to translocate and bind prosurvival Bcl-2 proteins. Thus, at least two mammalian BH3-only proteins, Bmf and Bim, function to sense intracellular damage by their localization to distinct cytoskeletal structures.

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Puthalakath, H., Huang, D. C. S., O'REILLY, L. A., King, S. M., & Strasser, A. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80456-6 · Cited by 1,053
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H. Puthalakath D. C. S. Huang L. A. O'Reilly
Supplementary material is available on Science Online at www.sciencemag.org/cgi/content/full/293/5536/1829/DC1
Wick W., et al., Oncogene 12, 973 (1996).
We thank L. O'Connor and K. Newton for help with experiments and sequence analysis L. Cullen and S. Novakovic for expert technical assistance J. Visvader and W. Alexander for reagents and G. Filby for editorial assistance. We are grateful to J. Adams P. Bouillet A. Harris and S. Cory for critical review of the manuscript. This work was supported by fellowships and grants from the National Health and Medical Research Council (Canberra; Reg. Key 973002) the U.S. National Cancer Institute (CA 80188) the Dr Josef Steiner Cancer Research Foundation the Leukemia and Lymphoma Society of America the Human Frontiers Science Program and the Sylvia and Charles Viertel Charitable Foundation. The sequences for mouse bmf human bmf and mouse dlc 2 have been deposited with GenBank (accession numbers: and respectively).

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Keane, O. M., Zadissa, A., Wilson, T. M., Hyndman, D. L., Greer, G. J., Baird, D., McCulloch, A., Crawford, A. M., & McEwan, J. C. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-42 · Cited by 94
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Vlahakis, A., & Debnath, J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.11.027 · Cited by 89
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Wang, Y., Srinivasan, K., Siddiqui, M. R., George, S. P., Tomar, A., & Khurana, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707962200 · Cited by 92
Molecular signaling regulating anchorage-independent growth of cancer cells.
Wang, L. (2004) · PubMed · Cited by 92
The NF-κB regulator Bcl-3 and the BH3-only proteins Bim and Puma control the death of activated T cells
Bauer, A., Villunger, A., Labi, V., Fischer, S. F., Strasser, A., Wagner, H., Schmid, R. M., & Häcker, G. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603625103 · Cited by 89
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Nollet, M., Hicks, H., McCarthy, A. P., Wu, H., Möller‐Levet, C. S., Laing, E., Malki, K., Lawless, N., Wafford, K. A., Dijk, D., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1816456116 · Cited by 95
Displacement of Bim by Bmf and Puma rather than increase in Bim level mediates paclitaxel-induced apoptosis in breast cancer cells
Kütük, Ö., & Letai, A. G. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.41 · Cited by 89
Cellular mechanisms of neuronal damage from hyperthermia
White, M. G., Luca, L. E., Nonner, D., Saleh, O., Hu, B. R., Barrett, E. F., & Barrett, J. N. (2007) · Progress in brain research · doi:10.1016/s0079-6123(06)62017-7 · Cited by 87
Involvement of BCL2 family members in the regulation of human oocyte and early embryo survival and death: gene expression and beyond
Boumela, I., Assou, S., Aouacheria, A., Haouzi, D., Déchaud, H., Vos, J. D., Handyside, A. H., & Hamamah, S. (2011) · Reproduction · doi:10.1530/rep-10-0504 · Cited by 89
Free radicals and apoptosis: relationships with glutathione, thioredoxin and the BCL family of proteins
Julie, C.-M. (2005) · Frontiers in bioscience · doi:10.2741/1656 · Cited by 89
Cell death as a result of calcium signaling modulation: A cancer-centric prospective
Danese, A., Leo, S., Rimessi, A., Wieckowski, M. R., Fiorica, F., Giorgi, C., & Pinton, P. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119061 · Cited by 91
Chronic lymphocytic leukemia cells display p53-dependent drug-induced Puma upregulation
Mackus, W. J. M., Kater, A. P., Grummels, A., Evers, L. M., Hooijbrink, B., Kramer, M. H. H., Castro, J. E., Kipps, T. J., van Lier, R. A. W., van Oers, M. H. J., et al. (2005) · Leukemia · doi:10.1038/sj.leu.2403623 · Cited by 87
Biological aspects of signal transduction by cell adhesion receptors
Alahari, S. K., Reddig, P. J., & Juliano, R. L. (2002) · International review of cytology · doi:10.1016/s0074-7696(02)20005-4 · Cited by 88
Anti-proliferative and pro-apoptotic effect of Smilax glabra Roxb. extract on hepatoma cell lines
Sa, F., Gao, J., Fung, K., Zheng, Y., Lee, S. M., & Wang, Y. (2007) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2007.08.012 · Cited by 87
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Tesfaigzi, Y. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0014oc · Cited by 88
Apoptosis in amyotrophic lateral sclerosis—what is the evidence?
Sathasivam, S., & Shaw, P. J. (2005) · The Lancet Neurology · doi:10.1016/s1474-4422(05)70142-3 · Cited by 86
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de Graauw, M., Tijdens, I. B., Cramer, R., Corless, S., Timms, J. F., & van de Water, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412708200 · Cited by 86
Carcinogenesis and apoptosis: paradigms and paradoxes
Zhivotovsky, B. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl035 · Cited by 85
The small GTPase Rac1 is a novel binding partner of Bcl-2 and stabilizes its antiapoptotic activity
Velaithan, R., Kang, J., Hirpara, J. L., Loh, T. K. S., Goh, B. C., Bras, M. L., Brenner, C., Clement, M., & Pervaiz, S. (2011) · Blood · doi:10.1182/blood-2010-08-301283 · Cited by 87
Cell Detachment Triggers p38 Mitogen-activated Protein Kinase-dependent Overexpression of Fas Ligand
Rosen, K. V., Shi, W., Calabretta, B., & Filmus, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207883200 · Cited by 83
The African swine fever virus dynein‐binding protein p54 induces infected cell apoptosis
Hernáez, B., Díaz‐Gil, G., Garcı́a-Gallo, M., Quetglas, J. I., Rodríguez‐Crespo, I., Dixon, L. K., Escribano, J. M., & Alonso, C. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.06.001 · Cited by 83
Intrinsically Disordered Proteins in Bcl-2 Regulated Apoptosis
Rautureau, G. J. P., Day, C. L., & Hinds, M. G. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11041808 · Cited by 91
Fish as model systems for the study of vertebrate apoptosis
Krumschnabel, G., & Podrabsky, J. E. (2008) · APOPTOSIS · doi:10.1007/s10495-008-0281-y · Cited by 82
High expression of Bfl‐1 contributes to the apoptosis resistant phenotype in B‐cell chronic lymphocytic leukemia
Morales, A. A., Olsson, A., Celsing, F., Österborg, A., Jondal, M., & Osorio, L. M. (2004) · International Journal of Cancer · doi:10.1002/ijc.20614 · Cited by 81
A review of the role of Puma, Noxa and Bim in the tumorigenesis, therapy and drug resistance of chronic lymphocytic leukemia
Zhang, L.-N., Li, J., & Xu, W. (2012) · Cancer Gene Therapy · doi:10.1038/cgt.2012.84 · Cited by 84
The sensors and regulators of cell–matrix surveillance in anoikis resistance of tumors
Nagaprashantha, L. D., Vatsyayan, R., Lelsani, P. C. R., Awasthi, S., & Singhal, S. S. (2010) · International Journal of Cancer · doi:10.1002/ijc.25725 · Cited by 84

Authors: Puthalakath, H., Villunger, A., O'Reilly, L. A., Beaumont, J. G., Coultas, L., Cheney, R. E., Huang, D. C. S., & Strasser, A.
Affiliations: The Royal Melbourne Hospital (AU)
The Walter and Eliza Hall Institute of Medical Research, Melbourne, P.O. Royal Melbourne Hospital, 3050 VIC, Australia.
University of North Carolina at Chapel Hill (US)
Corresponding author: Strasser, Andreas
ORCID: Puthalakath, Hamsa
Villunger, Andreas
Coultas, Leigh
Cheney, Richard E.
Huang, David C. S.
Strasser, Andreas
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2001-09-07
Volume: 293
Issue: 5536
Pages: 1829-1832
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1062257
OpenAlex: W1993059855
Cited by: 656
References: 24
Citations by year: 2026: 8 · 2025: 10 · 2024: 13 · 2023: 16 · 2022: 12 · 2021: 41 · 2020: 10 · 2019: 15 · 2018: 15 · 2017: 13 · 2016: 18 · 2015: 23 · 2014: 14 · 2013: 25 · 2012: 27
FWCI: 15.63
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (#CA 80188, R01CA080188)
National Institute on Deafness and Other Communication Disorders (R29DC003299)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: BMF, BH3-only proteins, apoptosis, myosin V, anoikis, Bcl-2 family proteins, cytoskeleton, building information modeling, protein translocation
MeSH terms: Bcl-2-Like Protein 11, Amino Acid Sequence, Animals, Calmodulin-Binding Proteins, Carrier Proteins, Cell Line, Cytoskeleton, Dyneins, Humans, Membrane Proteins, Molecular Sequence Data, Mutation, Neoplasm Proteins, Nerve Tissue Proteins, Protein Binding, Proto-Oncogene Proteins, RNA, Messenger, Transfection, Protein Structure, Tertiary, Proto-Oncogene Proteins c-bcl-2, Molecular Motor Proteins, Two-Hybrid System Techniques, Gene Expression Profiling, Protein Transport, Anoikis, Myosin Type V, Drosophila Proteins, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, Mice, Myeloid Cell Leukemia Sequence 1 Protein

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Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis

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