A mitochondrial megachannel resides in monomeric F1FO ATP synthase

Nelli Mnatsakanyan; Marc C. Llaguno; Youshan Yang; Yangyang Yan; Joachim Weber; Fred J. Sigworth; Elizabeth A. Jonas

doi:10.1038/s41467-019-13766-2

Nature Communications (Dec 2019)

A mitochondrial megachannel resides in monomeric F1FO ATP synthase

Nelli Mnatsakanyan,
Marc C. Llaguno,
Youshan Yang,
Yangyang Yan,
Joachim Weber,
Fred J. Sigworth,
Elizabeth A. Jonas

Affiliations

Nelli Mnatsakanyan: Section of Endocrinology, Department of Internal Medicine, Yale University
Marc C. Llaguno: Center for Cellular and Molecular Imaging, Yale University
Youshan Yang: Department of Cellular and Molecular Physiology, Yale University
Yangyang Yan: Department of Cellular and Molecular Physiology, Yale University
Joachim Weber: Department of Chemistry and Biochemistry, Texas Tech University
Fred J. Sigworth: Department of Cellular and Molecular Physiology, Yale University
Elizabeth A. Jonas: Section of Endocrinology, Department of Internal Medicine, Yale University

DOI: https://doi.org/10.1038/s41467-019-13766-2
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 11

Abstract

Read online

The ATP synthase has been suggested to contain the mitochondrial permeability transition pore (mPTP), which has a crucial role in cell death. Here the authors show that reconstituted ATP synthase monomers form voltage-gated and Ca2+ -activated channels with the key features of mPTP.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal