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The mitochondrial permeability transition (PT) is a Ca 2+ -dependent permeability increase of the inner mitochondrial membrane mediated by opening of a high-conductance channel, the PT pore. Its molecular nature has been the subject of intense research and the source of controversies, but a considerable consensus has been reached that the PT originates from specific conformations of the F O F 1 -ATP synthase and of the adenine nucleotide translocator. The ATP synthase forms high-conductance channels in mammals and yeast but not in the anoxia- and salt-tolerant brine shrimp Artemia franciscana , which is refractory to the PT; it forms low-conductance and Ca 2+ -selective channels in Drosophila melanogaster , which undergoes a process of Ca 2+ -induced Ca 2+ release but not a PT. The structural definition of ATP synthases from several species may allow for some inferences to be made about the mechanism of channel formation, or lack thereof, and provides a testable framework for future research.
Carraro et al. (Fri,) studied this question.