The mitochondrial permeability transition: Recent progress and open questions.

Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1742-4658 (Electronic) Linking ISSN: 1742464X NLM ISO Abbreviation: FEBS J Subsets: MEDLINE

Original Publication: Oxford, UK : Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies, c2005-

Mitochondrial Transmembrane Permeability-Driven Necrosis* ; Mitochondrial Permeability Transition Pore*; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Proton-Translocating ATPases/genetics ; Mitochondrial Proton-Translocating ATPases/metabolism ; Permeability ; Adenosine Triphosphate/metabolism ; Calcium/metabolism

Major progress has been made in defining the basis of the mitochondrial permeability transition, a Ca ²⁺ -dependent permeability increase of the inner membrane that has puzzled mitochondrial research for almost 70 years. Initially considered an artefact of limited biological interest by most, over the years the permeability transition has raised to the status of regulator of mitochondrial ion homeostasis and of druggable effector mechanism of cell death. The permeability transition is mediated by opening of channel(s) modulated by matrix cyclophilin D, the permeability transition pore(s) (PTP). The field has received new impulse (a) from the hypothesis that the PTP may originate from a Ca ²⁺ -dependent conformational change of F-ATP synthase and (b) from the reevaluation of the long-standing hypothesis that it originates from the adenine nucleotide translocator (ANT). Here, we provide a synthetic account of the structure of ANT and F-ATP synthase to discuss potential and controversial mechanisms through which they may form high-conductance channels; and review some intriguing findings from the wealth of early studies of PTP modulation that still await an explanation. We hope that this review will stimulate new experiments addressing the many outstanding problems, and thus contribute to the eventual solution of the puzzle of the permeability transition.
(© 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

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Keywords: ATP synthase; adenine nucleotide translocator; calcium transport; channels; cyclophilin; cyclosporine; mitochondria; permeability transition

0 (Mitochondrial Permeability Transition Pore)
0 (Mitochondrial Membrane Transport Proteins)
EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
8L70Q75FXE (Adenosine Triphosphate)
SY7Q814VUP (Calcium)

Date Created: 20211028 Date Completed: 20221116 Latest Revision: 20230111

20230112

PMC9787756

10.1111/febs.16254

34710270