The mitochondrial permeability transition from yeast to mammals
Abstract
Regulated permeability changes have been detected in mitochondria across species. We review here their key features, with the goal of assessing whether a “permeability transition” similar to that observed in higher eukaryotes is present in other species. The recent discoveries (i) that treatment with cyclosporin A (CsA) unmasks an inhibitory site for inorganic phosphate (Pi) [Basso, E., Petronilli, V., Forte, M.A. and Bernardi, P. (2008) Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation. J. Biol. Chem. 283, 26307–26311], the classical inhibitor of the permeability transition of yeast and (ii) that under proper experimental conditions a matrix Ca2+-dependence can be demonstrated in yeast as well [Yamada, A., Yamamoto, T., Yoshimura, Y., Gouda, S., Kawashima, S., Yamazaki, N., Yamashita, K., Kataoka, M., Nagata, T., Terada, H., Pfeiffer, D.R. and Shinohara Y. (2009) Ca2+-induced permeability transition can be observed even in yeast mitochondria under optimized experimental conditions. Biochim. Biophys. Acta 1787, 1486–1491] suggest that the mitochondrial permeability transition has been conserved during evolution.
Abbreviations: ANT, adenine nucleotide translocator, CsA, cyclosporin A, CyP, cyclophilin, IMM, inner mitochondrial membrane, NEM, N-ethylmaleimide, OMM, outer mitochondrial membrane, Pi, inorganic phosphate, PT, permeability transition, PTP, permeability transition pore, VDAC, voltage-dependent anion channel, YMUC, yeast mitochondrial unselective channel
Keywords: Mitochondria, Permeability transition, Calcium, Cyclosporin, Cyclophilin
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PII: S0014-5793(10)00293-0
doi:10.1016/j.febslet.2010.04.023
© 2010 Federation of European Biochemical Societies
