Cell death disguised: The mitochondrial permeability transition pore as the c-subunit of the F1FO ATP synthase

Elizabeth A. Jonas, George A. Porter, Gisela Beutner, Nelli Mnatsakanyan, Kambiz N. Alavian

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

Abstract

Ion transport across the mitochondrial inner and outer membranes is central to mitochondrial function, including regulation of oxidative phosphorylation and cell death. Although essential for ATP production by mitochondria, recent findings have confirmed that the c-subunit of the ATP synthase also houses a large conductance uncoupling channel, the mitochondrial permeability transition pore (mPTP), the persistent opening of which produces osmotic dysregulation of the inner mitochondrial membrane and cell death. This review will discuss recent advances in understanding the molecular components of mPTP, its regulatory mechanisms and how these contribute directly to its physiological as well as pathological roles.

Original languageEnglish (US)
Pages (from-to)382-392
Number of pages11
JournalPharmacological Research
Volume99
DOIs
StatePublished - Sep 3 2015

All Science Journal Classification (ASJC) codes

  • Pharmacology

Fingerprint

Dive into the research topics of 'Cell death disguised: The mitochondrial permeability transition pore as the c-subunit of the F1FO ATP synthase'. Together they form a unique fingerprint.

Cite this