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- W3043136578 endingPage "105081" @default.
- W3043136578 startingPage "105081" @default.
- W3043136578 abstract "• ATP synthase as the mitochondrial permeability transition pore. • Subunit e of the membrane bending F o domain likely involved in channel gating. • Working model of c-ring as pore forming domain. • Comparison to lipid mediated channel closure in gap junctions. • Cristae architecture and oligomeric state as master controller of pore opening. The current state of research on the mitochondrial permeability transition pore (PTP) can be described in terms of three major problems: molecular identity, atomic structure and gating mechanism. In this review these three problems are discussed in the light of recent findings with special emphasis on the discovery that the PTP is mitochondrial F-ATP synthase (mtF o F 1 ). Novel features of the mitochondrial F-ATP synthase emerging from the success of single particle cryo electron microscopy (cryo-EM) to determine F-ATP synthase structures are surveyed along with their possible involvement in pore formation. Also, current findings from the gap junction field concerning the involvement of lipids in channel closure are examined. Finally, an earlier proposal denoted as the 'Death Finger' is discussed as a working model for PTP gating." @default.
- W3043136578 created "2020-07-23" @default.
- W3043136578 creator A5026204388 @default.
- W3043136578 date "2020-10-01" @default.
- W3043136578 modified "2023-09-29" @default.
- W3043136578 title "Mitochondrial F-ATP synthase as the permeability transition pore" @default.
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