title: Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition.
abstract: The term mitochondrial permeability transition (MPT) is commonly used to indicate an abrupt increase in the permeability of the inner mitochondrial membrane to low molecular weight solutes. Widespread MPT has catastrophic consequences for the cell, de facto marking the boundary between cellular life and death. MPT results indeed in the structural and functional collapse of mitochondria, an event that commits cells to suicide via regulated necrosis or apoptosis. MPT has a central role in the etiology of both acute and chronic diseases characterized by the loss of post-mitotic cells. Moreover, cancer cells are often relatively insensitive to the induction of MPT, underlying their increased resistance to potentially lethal cues. Thus, intense efforts have been dedicated not only at the understanding of MPT in mechanistic terms, but also at the development of pharmacological MPT modulators. In this setting, multiple mitochondrial and extramitochondrial proteins have been suspected to critically regulate the MPT. So far, however, only peptidylprolyl isomerase F (best known as cyclophilin D) appears to constitute a key component of the so-called permeability transition pore complex (PTPC), the supramolecular entity that is believed to mediate MPT. Here, after reviewing the structural and functional features of the PTPC, we summarize recent findings suggesting that another of its core components is represented by the c subunit of mitochondrial ATP synthase.
authors.affiliation: Section of Pathology, Oncology and Experimental Biology, Laboratory for Technologies of Advanced Therapies (LTTA), Department of Morphology, Surgery and Experimental Medicine, Interdisciplinary Centre for the Study of Inflammation (ICSI), University of Ferrara, Ferrara, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Bonora
authors.affiliation: Department of Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
authors.forename: M R
authors.initials: MR
authors.lastname: Wieckowski
authors.affiliation: Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary.
authors.forename: C
authors.initials: C
authors.lastname: Chinopoulos
authors.affiliation: 1] Equipe 11 labelisée par la Ligue Nationale contre le cancer, INSERM U1138, Centre de Recherche des Cordeliers, Paris, France [2] Université Paris Descartes/Paris 5, Sorbonne Paris Cité, Paris, France [3] Metabolomics and Cell Biology platforms, Gustave Roussy Comprehensive Cancer Center, Villejuif, France.
authors.forename: O
authors.initials: O
authors.lastname: Kepp
authors.affiliation: 1] Equipe 11 labelisée par la Ligue Nationale contre le cancer, INSERM U1138, Centre de Recherche des Cordeliers, Paris, France [2] Université Paris Descartes/Paris 5, Sorbonne Paris Cité, Paris, France [3] Metabolomics and Cell Biology platforms, Gustave Roussy Comprehensive Cancer Center, Villejuif, France [4] Pôle de Biologie, Hôpital Européen Georges Pompidou, AP-HP, Paris, France.
authors.forename: G
authors.initials: G
authors.lastname: Kroemer
authors.affiliation: 1] Equipe 11 labelisée par la Ligue Nationale contre le cancer, INSERM U1138, Centre de Recherche des Cordeliers, Paris, France [2] Université Paris Descartes/Paris 5, Sorbonne Paris Cité, Paris, France [3] Gustave Roussy Comprehensive Cancer Center, Villejuif, France.
authors.forename: L
authors.initials: L
authors.lastname: Galluzzi
authors.affiliation: Section of Pathology, Oncology and Experimental Biology, Laboratory for Technologies of Advanced Therapies (LTTA), Department of Morphology, Surgery and Experimental Medicine, Interdisciplinary Centre for the Study of Inflammation (ICSI), University of Ferrara, Ferrara, Italy.
authors.forename: P
authors.initials: P
authors.lastname: Pinton
mesh_terms: D000818:Animals; D016923:Cell Death; D002463:Cell Membrane Permeability; D000081406:Peptidyl-Prolyl Isomerase F; D021983:Cyclophilins / Q000378:metabolism; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D033681:Mitochondrial Membrane Transport Proteins / Q000378:metabolism; D051336:Mitochondrial Membranes / Q000378:metabolism*; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000081406:Peptidyl-Prolyl Isomerase F; D033681:Mitochondrial Membrane Transport Proteins; D025261:Mitochondrial Proton-Translocating ATPases; D021983:Cyclophilins
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