What Makes You Can also Break You, Part III: Mitochondrial Permeability Transition Pore Formation by an Uncoupling Channel within the C-Subunit Ring of the F1FO ATP Synthase?

Christos Chinopoulos,Gyorgy Szabadkai

doi:10.3389/fonc.2014.00235

Christos Chinopoulos, Gyorgy Szabadkai

Open Access

https://doi.org/10.3389/fonc.2014.00235

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Abstract

What Makes You Can also Break You, Part III: Mitochondrial Permeability Transition Pore Formation by an Uncoupling Channel within the C-Subunit Ring of the F1FO ATP Synthase?

Highlights

An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore by Alavian KN, Beutner G, Lazrove E, Sacchetti S, Park HA, Licznerski P, Li H, Nabili P, Hockensmith K, Graham M, Porter GA Jr., Jonasa EA
In the hunt for identifying the structural elements of the mitochondrial transition pore, the recent paper by Alavian et al proposes that the pore is formed by an uncoupling channel within the c-subunit ring of the F1FO ATP-synthase complex [1], reaffirming previous results [2, 3] and providing exciting additional details about the potential molecular mechanism controlling pore formation
Channel activity matched that of the mitochondrial megachannel, known as being the permeability transition pore (PTP) [4]

Summary

Introduction

An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore by Alavian KN, Beutner G, Lazrove E, Sacchetti S, Park HA, Licznerski P, Li H, Nabili P, Hockensmith K, Graham M, Porter GA Jr., Jonasa EA. In the hunt for identifying the structural elements of the mitochondrial transition pore, the recent paper by Alavian et al proposes that the pore is formed by an uncoupling channel within the c-subunit ring of the F1FO ATP-synthase complex [1], reaffirming previous results [2, 3] and providing exciting additional details about the potential molecular mechanism controlling pore formation.

Results

Conclusion