What Makes You Can Also Break You, Part II: Mitochondrial Permeability Transition Pore Formation by Dimers of the F1FO ATP-Synthase?

Gyorgy Szabadkai,Christos Chinopoulos

doi:10.3389/fonc.2013.00140

Abstract

What Makes You Can Also Break You, Part II: Mitochondrial Permeability Transition Pore Formation by Dimers of the F1FO ATP-Synthase?

Highlights

A few months ago we commented on the findings by Bonora et al (2013), regarding the role of the c ring of the F1FO ATP synthase forming the mitochondrial permeability transition
Following a long debate of the presumed components cyclophilin D emerged as an essential regulator and a bona fide component associated with the actual pore
Giorgio et al (2013) show that by incorporating purified F1FO ATP-synthase dimers in liposomes, electrophysiological recordings identical to the mitochondrial megachannel” (MMC) can be obtained. Whilst these results provide the most direct evidence so far for mitochondrial permeability transition (mPT) pore formation by the F1FO ATP-synthase, again, they raise a series of new questions

Summary

Introduction

A few months ago we commented on the findings by Bonora et al (2013), regarding the role of the c ring of the F1FO ATP synthase forming the mitochondrial permeability transition (mPT). The present work characterizes the cypD – F1FO ATP-synthase interaction from the point of view of mPT formation, providing evidence that cypD targets the OSCP subunit of the lateral stalk. In addition to presenting a series of biochemical and functional evidence indicating that the mPT is correlated with the cypD-OSCP interaction, they directly addressed the pore forming ability of purified F1FO ATP-synthases.

Results

Conclusion