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Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore.

Abstract：

:The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. By combining highly purified, fully active bovine F-ATP synthase with preformed liposomes we show that Ca2+ dissipates the H+ gradient generated by ATP hydrolysis. After incorporation of the same preparation into planar lipid bilayers Ca2+ elicits currents matching those of the MMC/PTP. Currents were fully reversible, were stabilized by benzodiazepine 423, a ligand of the OSCP subunit of F-ATP synthase that activates the MMC/PTP, and were inhibited by Mg2+ and adenine nucleotides, which also inhibit the PTP. Channel activity was insensitive to inhibitors of the adenine nucleotide translocase (ANT) and of the voltage-dependent anion channel (VDAC). Native gel-purified oligomers and dimers, but not monomers, gave rise to channel activity. These findings resolve the long-standing mystery of the MMC/PTP and demonstrate that Ca2+ can transform the energy-conserving F-ATP synthase into an energy-dissipating device.

journal_name

Nat Commun

journal_title

Nature communications

authors

Urbani A,Giorgio V,Carrer A,Franchin C,Arrigoni G,Jiko C,Abe K,Maeda S,Shinzawa-Itoh K,Bogers JFM,McMillan DGG,Gerle C,Szabò I,Bernardi P

doi

10.1038/s41467-019-12331-1

subject

Has Abstract

pub_date

2019-09-25 00:00:00

pages

4341

issue

1

issn

2041-1723

pii

10.1038/s41467-019-12331-1

journal_volume

10

pub_type

杂志文章

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