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Cited by 458

The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.

Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition

Open access
Bonora, Massimo, Bononi, Angela, De Marchi, Elena, Giorgi, Carlotta, Lebiedzinska, Magdalena, Marchi, Saverio, Patergnani, Simone, Rimessi, Alessandro, Suski, Jan M., Wojtala, Aleksandra, Wieckowski, Mariusz R., Kroemer, Guido, Galluzzi, Lorenzo, Pinton, Paolo·2013·Cell Cycle

Abstract

The term "mitochondrial permeability transition" (MPT) refers to an abrupt increase in the permeability of the inner mitochondrial membrane to low molecular weight solutes. Due to osmotic forces, MPT is paralleled by a massive influx of water into the mitochondrial matrix, eventually leading to the structural collapse of the organelle. Thus, MPT can initiate mitochondrial outer membrane permeabilization (MOMP), promoting the activation of the apoptotic caspase cascade as well as of caspase-independent cell death mechanisms. MPT appears to be mediated by the opening of the so-called "permeability transition pore complex" (PTPC), a poorly characterized and versatile supramolecular entity assembled at the junctions between the inner and outer mitochondrial membranes. In spite of considerable experimental efforts, the precise molecular composition of the PTPC remains obscure and only one of its constituents, cyclophilin D (CYPD), has been ascribed with a crucial role in the regulation of cell death. Conversely, the results of genetic experiments indicate that other major components of the PTPC, such as voltage-dependent anion channel (VDAC) and adenine nucleotide translocase (ANT), are dispensable for MPT-driven MOMP. Here, we demonstrate that the c subunit of the FO ATP synthase is required for MPT, mitochondrial fragmentation and cell death as induced by cytosolic calcium overload and oxidative stress in both glycolytic and respiratory cell models. Our results strongly suggest that, similar to CYPD, the c subunit of the FO ATP synthase constitutes a critical component of the PTPC.

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Metadata

Authors
Bonora, M., Bononi, A., De Marchi, E., Giorgi, C., Lebiedzinska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., Wieckowski, M. R., Kroemer, G., Galluzzi, L., & Pinton, P.
Venue
Cell Cycle
Published
2013-01-23
Volume
12
Issue
4
Pages
674-683
ISSN
  • 1538-4101 (ISSN-L)
  • 1551-4005
OpenAlex
W1993418135
Cited by
458
References
73
FWCI
22.46
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition. https://app.cochat.ai/papers/10.4161/cc.23599
The paper
Bonora, M., Bononi, A., De Marchi, E., Giorgi, C., Lebiedzinska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., Wieckowski, M. R., Kroemer, G., Galluzzi, L., & Pinton, P. (2013). Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition. Cell Cycle. https://doi.org/10.4161/cc.23599

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.