The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Oligomerization of the Mitochondrial Protein Voltage-Dependent Anion Channel Is Coupled to the Induction of Apoptosis
Open accessAbstract
Accumulating evidence implicates that the voltage-dependent anion channel (VDAC) functions in mitochondrion-mediated apoptosis and as a critical player in the release of apoptogenic proteins, such as cytochrome c, triggering caspase activation and apoptosis. The mechanisms regulating cytochrome c release and the molecular architecture of the cytochrome c-conducting channel remain unknown. Here the relationship between VDAC oligomerization and the induction of apoptosis was examined. We demonstrated that apoptosis induction by various stimuli was accompanied by highly increased VDAC oligomerization, as revealed by cross-linking and directly monitored in living cells using bioluminescence resonance energy transfer technology. VDAC oligomerization was induced in all cell types and with all apoptosis inducers used, including staurosporine, curcumin, As(2)O(3), etoposide, cisplatin, selenite, tumor necrosis factor alpha (TNF-α), H(2)O(2), and UV irradiation, all acting through different mechanisms yet all involving mitochondria. Moreover, correlation between the levels of VDAC oligomerization and apoptosis was observed. Furthermore, the apoptosis inhibitor 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) inhibited VDAC oligomerization. Finally, a caspase inhibitor had no effect on VDAC oligomerization and cytochrome c release. We propose that VDAC oligomerization is involved in mitochondrion-mediated apoptosis and may represent a general mechanism common to numerous apoptogens acting via different initiating cascades. Thus, targeting the oligomeric status of VDAC, and hence apoptosis, offers a therapeutic strategy for combating cancers and neurodegenerative diseases.
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Cites
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Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
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Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane
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Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
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Cytochrome c release from mitochondria proceeds by a two-step process
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Chemopreventive and therapeutic effects of curcumin
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VDAC, a multi-functional mitochondrial protein regulating cell life and death
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Self-citationAntonsson, B., Montessuit, S., Sanchez, B., & Martinou, J.-C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010810200 · Cited by 676
Cited by
VDAC oligomers form mitochondrial pores to release mtDNA fragments and promote lupus-like disease
Kim, J., Gupta, R., Blanco, L. P., Yang, S., Shteinfer-Kuzmine, A., Wang, K., Zhu, J., Yoon, H. E., Wang, X., Kerkhofs, M., et al. (2019) · Science · doi:10.1126/science.aav4011 · Cited by 793
Self-citationVDAC1, mitochondrial dysfunction, and Alzheimer’s disease
Shoshan-Barmatz, V., Nahon-Crystal, E., Shteinfer-Kuzmine, A., & Gupta, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.03.010 · Cited by 286
Self-citationLee, K., Kerner, J., & Hoppel, C. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228692 · Cited by 254
VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress
Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170
Self-citationBen-Hail, D., Begas-Shvartz, R., Shalev, M., Shteinfer-Kuzmine, A., Gruzman, A., Reina, S., De Pinto, V., & Shoshan-Barmatz, V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744284 · Cited by 158
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Metadata
- Authors
- Keinan, N., Tyomkin, D., & Shoshan-Barmatz, V.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2010-12-01
- Volume
- 30
- Issue
- 24
- Pages
- 5698-5709
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2163630562
- Cited by
- 264
- References
- 65
- FWCI
- 4.49
- Type
- journal article
- Language
- en
- Open access
- green
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