Novel insights into the mitochondrial permeability transition

Massimo Bonora, José Manuel Bravo-San Pedro, Guido Kroemer, Lorenzo Galluzzi, Paolo Pinton

Research output: Contribution to journalReview articlepeer-review

21 Scopus citations

Abstract

Alavian and colleagues recently provided further evidence in support of the notion that the c subunit of the mitochondrial F1FO ATP synthase constitutes the long-sought pore-forming unit of the supramolecular complex responsible for the so-called 'mitochondrial permeability transition' (MPT). Besides shedding new light on the molecular mechanisms that underlie the MPT, these findings corroborate the notion that several components of the cell death machinery, including cytochrome c and the F1FO ATP synthase, mediate critical metabolic activities.

Original languageEnglish
Pages (from-to)2666-2670
Number of pages5
JournalCell Cycle
Volume13
Issue number17
DOIs
StatePublished - Sep 1 2014
Externally publishedYes

Keywords

  • Apoptosis
  • BCL-X
  • Cyclophilin D
  • Cyclosporin A
  • Necrosis
  • Permeability transition pore complex

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