Abstract
The C Ring of the F1Fo ATP Synthase Forms the Mitochondrial Permeability Transition Pore: A Critical Appraisal.
Highlights
An uncoupling channel within the csubunit 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
The mitochondrial permeability transition pore (MPTP) is a non-specific pore in the inner mitochondrial membrane (IMM) whose opening is triggered by high matrix [Ca2+] to which it is sensitized by [Pi] and oxidative stress
Liver mitochondria lacking ANT1 and ANT2 exhibit MPTP opening that is insensitive to adenine nucleotides, CAT and BKA, and requires higher [Ca2+]
Summary
An uncoupling channel within the csubunit 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. The ANT binds CyP-D and, when reconstituted into proteoliposomes, it produces Ca2+activated pores similar to the MPTP [6, 7]. The available data suggest that the ANT and PiC play roles in MPTP opening but that another IMM protein must be involved.
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