The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Tubulin Is an Inherent Component of Mitochondrial Membranes That Interacts with the Voltage-dependent Anion Channel
Open accessAbstract
We have previously reported that anti-tubulin agents induce the release of cytochrome c from isolated mitochondria. In this study, we show that tubulin is present in mitochondria isolated from different human cancerous and non-cancerous cell lines. The absence of polymerized microtubules and cytosolic proteins was checked to ensure that this tubulin is an inherent component of the mitochondria. In addition, a salt wash did not release the tubulin from the mitochondria. By using electron microscopy, we then showed that tubulin is localized in the mitochondrial membranes. As compared with cellular tubulin, mitochondrial tubulin is enriched in acetylated and tyrosinated alpha-tubulin and is also enriched in the class III beta-tubulin isotype but contains very little of the class IV beta-tubulin isotype. The mitochondrial tubulin is likely to be organized in alpha/beta dimers and represents 2.2 +/- 0.5% of total cellular tubulin. Lastly, we showed by immunoprecipitation experiments that the mitochondrial tubulin is specifically associated with the voltage-dependent anion channel, the main component of the permeability transition pore. Thus, tubulin is an inherent component of mitochondrial membranes, and it could play a role in apoptosis via interaction with the permeability transition pore.
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Cites
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Organelle-specific initiation of cell death pathways
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A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis
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The mitochondrion in apoptosis: how Pandora's box opens
Zamzami, N., & Kroemer, G. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35048073 · Cited by 1,028
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Mitochondria--the Death Signal Integrators
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The Golgi Complex Is a Microtubule-organizing Organelle
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Resistance to Taxol in lung cancer cells associated with increased microtubule dynamics
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Self-citationThe voltage-dependent anion channel: an essential player in apoptosis
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Cited by
Shen, S., Li, X.-F., Cullen, W. R., Weinfeld, M., & Le, X. C. (2013) · Chemical Reviews · doi:10.1021/cr300015c · Cited by 818
Microtubules, microtubule-interfering agents and apoptosis
Mollinedo, F., & Gajate, C. (2003) · Apoptosis · doi:10.1023/a:1025513106330 · Cited by 477
Microtubules and Their Role in Cellular Stress in Cancer
Parker, A. L., Kavallaris, M., & McCarroll, J. A. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00153 · Cited by 440
Chemotherapy-induced peripheral neuropathy: What do we know about mechanisms?
Carozzi, V. A., Canta, A., & Chiorazzi, A. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2014.10.014 · Cited by 431
Tubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration
Rostovtseva, T. K., Sheldon, K. L., Hassanzadeh, E., Monge, C., Saks, V., Bezrukov, S. M., & Sackett, D. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806303105 · Cited by 366
Metadata
- Authors
- Carreá, M., Andreá, N., Carles, G., Borghi, H., Brichese, L., Briand, C., & Braguer, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-09
- Volume
- 277
- Issue
- 37
- Pages
- 33664-33669
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2056775926
- Cited by
- 273
- References
- 28
- FWCI
- 2.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Carreá, M., Andreá, N., Carles, G., Borghi, H., Brichese, L., Briand, C., & Braguer, D. (2002). Tubulin Is an Inherent Component of Mitochondrial Membranes That Interacts with the Voltage-dependent Anion Channel. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m203834200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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