Unknown

Dataset Information

0

Cell death disguised: The mitochondrial permeability transition pore as the c-subunit of the F(1)F(O) ATP synthase.


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.

SUBMITTER: Jonas EA 

PROVIDER: S-EPMC4567435 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cell death disguised: The mitochondrial permeability transition pore as the c-subunit of the F(1)F(O) ATP synthase.

Jonas Elizabeth A EA   Porter George A GA   Beutner Gisela G   Mnatsakanyan Nelli N   Alavian Kambiz N KN  

Pharmacological research 20150505


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  ...[more]

Similar Datasets

| S-EPMC3625323 | biostudies-literature
| S-EPMC5494526 | biostudies-literature
| S-EPMC1220352 | biostudies-other
| S-EPMC5380099 | biostudies-literature
| S-EPMC3594268 | biostudies-other