FEBS Letters
Volume 584, Issue 12 , Pages 2504-2509, 18 June 2010

The mitochondrial permeability transition from yeast to mammals

Edited by Jan Rydström

  • Luca Azzolin

      Affiliations

    • Department of Biomedical Sciences, CNR Institute of Neuroscience, University of Padova, Italy
  • ,
  • Sophia von Stockum

      Affiliations

    • Department of Biomedical Sciences, CNR Institute of Neuroscience, University of Padova, Italy
  • ,
  • Emy Basso

      Affiliations

    • Department of Biomedical Sciences, CNR Institute of Neuroscience, University of Padova, Italy
  • ,
  • Valeria Petronilli

      Affiliations

    • Department of Biomedical Sciences, CNR Institute of Neuroscience, University of Padova, Italy
  • ,
  • Michael A. Forte

      Affiliations

    • Vollum Institute, Oregon Health and Sciences University, Portland, OR, USA
  • ,
  • Paolo Bernardi

      Affiliations

    • Department of Biomedical Sciences, CNR Institute of Neuroscience, University of Padova, Italy
    • Corresponding Author InformationCorresponding author. Address: Department of Biomedical Sciences, University of Padova, Viale Giuseppe Colombo 3, I-35121 Padova, Italy. Fax: +39 049 827 6361.

Received 4 March 2010; received in revised form 1 April 2010; accepted 9 April 2010. published online 14 April 2010.

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

FEBS Letters
Volume 584, Issue 12 , Pages 2504-2509, 18 June 2010