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Hexokinase-I Protection against Apoptotic Cell Death Is Mediated via Interaction with the Voltage-dependent Anion Channel-1
Open accessAbstract
In brain and tumor cells, the hexokinase isoforms HK-I and HK-II bind to the voltage-dependent anion channel (VDAC) in the outer mitochondrial membrane. We have previously shown that HK-I decreases murine VDAC1 (mVDAC1) channel conductance, inhibits cytochrome c release, and protects against apoptotic cell death. Now, we define mVDAC1 residues, found in two cytoplasmic domains, involved in the interaction with HK-I. Protection against cell death by HK-I, as induced by overexpression of native or mutated mVDAC1, served to identify the mVDAC1 amino acids required for interaction with HK-I. HK-I binding to mVDAC1 either in isolated mitochondria or reconstituted in a bilayer was inhibited upon mutation of specific VDAC1 residues. HK-I anti-apoptotic activity was also diminished upon mutation of these amino acids. HK-I-mediated inhibition of cytochrome c release induced by staurosporine was also diminished in cells expressing VDAC1 mutants. Our results thus offer new insights into the mechanism by which HK-I promotes tumor cell survival via inhibition of cytochrome c release through HK-I binding to VDAC1. These results, moreover, point to VDAC1 as a key player in mitochondrially mediated apoptosis and implicate an HK-I-VDAC1 interaction in the regulation of apoptosis. Finally, these findings suggest that interference with the binding of HK-I to mitochondria by VDAC1-derived peptides may offer a novel strategy by which to potentiate the efficacy of conventional chemotherapeutic agents.
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“The hexokinase isoform HK-I binds to the N-terminus of VDAC1 on the cytoplasmic side of the outer mitochondrial membrane and has been shown in both in vitro and in vivo systems to protect against apoptosis [105,106].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [106]
Citations
Cites
Cellular processing of platinum anticancer drugs
Wang, D., & Lippard, S. J. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1691 · Cited by 3,801
Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function
Wilson, J. E. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00241 · Cited by 1,085
Gottlob, K., Majewski, N., Kennedy, S., Kandel, E., Robey, R. B., & Hay, N. (2001) · Genes & Development · doi:10.1101/gad.889901 · Cited by 961
Mitochondrial Binding of Hexokinase II Inhibits Bax-induced Cytochrome c Release and Apoptosis
Pastorino, J. G., Shulga, N., & Hoek, J. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109950200 · Cited by 721
Mitochondrial creatine kinase in human health and disease
Schlattner, U., Tokarska-Schlattner, M., & Wallimann, T. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.09.004 · Cited by 641
VDAC: The channel at the interface between mitochondria and the cytosol
Colombini, M. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000009862.17396.8d · Cited by 500
AZOULAY-ZOHAR, H., ISRAELSON, A., ABU-HAMAD, S., & SHOSHAN-BARMATZ, V. (2004) · Biochemical Journal · doi:10.1042/bj20031465 · Cited by 408
Self-citationPastorino, J. G., Hoek, J. B., & Shulga, N. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1925 · Cited by 405
GINCEL, D., ZAID, H., & SHOSHAN-BARMATZ, V. (2001) · Biochemical Journal · doi:10.1042/bj3580147 · Cited by 396
Pedersen, P. L., Mathupala, S. P., Rempel, A., Geschwind, J. F., & Ko, Y. H. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00248-7 · Cited by 363
Research works printed but not linked: 5
- Rempel, 1996, Cancer Res., 56, 2468
- Nakashima, 1988, Cancer Res., 48, 913
- De Pinto, 2003, Ital. J. Biochem., 52, 17
- Fanciulli, 1994, Oncol. Res., 6, 405
- Oudard, 2004, Bull. Cancer, 91, E184
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Song, G., Lu, Q., Fan, H., Zhang, X., Ge, L., Tian, R., Wang, S., Feng, T., Pan, J., Feng, J., et al. (2019) · Arthritis Research & Therapy · doi:10.1186/s13075-019-1865-3 · Cited by 65
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Weh, E., Lutrzykowska, Z., Smith, A. J. H., Hager, H. M., Pawar, M. D., Wubben, T. J., & Besirli, C. G. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2638-2 · Cited by 60
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Sullivan, L. S., Koboldt, D. C., Bowne, S. J., Lang, S. H., Blanton, S. H., Cadena, E. D., Avery, C. E., Lewis, R. A., Webb-Jones, K., Wheaton, D. H., et al. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-15419 · Cited by 61
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Zaid, H., Talior‐Volodarsky, I., Antonescu, C. N., Liu, Z., & Klip, A. (2009) · Biochemical Journal · doi:10.1042/bj20081319 · Cited by 61
Zhang, G., Jiang, G., Wang, C., Zhong, K., Zhang, J., Xue, Q., Li, X., Jin, H. D., & Li, B. (2016) · Oncotarget · doi:10.18632/oncotarget.9943 · Cited by 60
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Shen, X. L., Zhang, Y., Xu, W., Liang, R., Zheng, J., Luo, Y., Wang, Y., & Huang, K. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.10.010 · Cited by 57
Wilde, B. R., Ye, Z., Lim, T.-Y., & Ayer, D. E. (2019) · eLife · doi:10.7554/elife.40199 · Cited by 57
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Metadata
- Authors
- Abu-Hamad, S., Zaid, H., Israelson, A., Nahon, E., & Shoshan-Barmatz, V.
- Affiliations
- Hospital for Sick Children (CA)
- University of California San Diego (US)
- Ben-Gurion University of the Negev (IL)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 283
- Issue
- 19
- Pages
- 13482-13490
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2054645758
- Cited by
- 278
- References
- 49
- Citations by year
- 2026: 14 · 2025: 18 · 2024: 12 · 2023: 16 · 2022: 15 · 2021: 16 · 2020: 17 · 2019: 13 · 2018: 14 · 2017: 14 · 2016: 9 · 2015: 6 · 2014: 18 · 2013: 16 · 2012: 16
- FWCI
- 8.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Keywords
- hexokinase 1, VDAC1, apoptosis, cytochrome c release, mitochondrial permeability transition, tumor cell survival, staurosporine, mitochondrial outer membrane
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cytosol, Gene Expression Regulation, Hexokinase, Humans, Molecular Sequence Data, Mutation, Protein Binding, Sequence Alignment, Conserved Sequence, Apoptosis, Cytochromes c, Protein Kinase Inhibitors, Voltage-Dependent Anion Channel 1, Mice
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