The mitochondrial permeability transition from yeast to mammals |
| |
Authors: | Luca Azzolin Emy Basso Michael A. Forte |
| |
Affiliation: | a Department of Biomedical Sciences, CNR Institute of Neuroscience, University of Padova, Italy b Vollum Institute, Oregon Health and Sciences University, Portland, OR, USA |
| |
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. |
| |
Keywords: | 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 |
本文献已被 ScienceDirect 等数据库收录! |
|