Channels of the Outer Membrane of Saccharomyces cerevisiae Mitochondria: Cooperation and Regulation

References

• Ahting, U., Thieffry, M., Engelhardt, H., Hegerl, R., Neupert, W., and Nussberger, S. 2001. Tom40, the pore-forming component of the proteinconducting TOM channel in the outer membrane of mitochondria. J. Cell Biol. 153:1151–1160.
   PubMedGoogle Scholar
• Ahting, U., Thun, C., Hegerl, R., Typke, D., Nargang, F. E., Neupert, W., and Nussberger, S. 1999. The TOM core complex: the general import pore of the outer membrane of mitochondria. J. Cell Biol. 147:959–968.
   Google Scholar
• Antos, N., Budzinska, M., and Kmita, H. 2001a. An interplay between the TOM complex and porin isoforms in the yeast Saccharomyces cerevisiae mitochondria. FEBS Lett. 500:12–16.
   PubMedGoogle Scholar
• Antos, N., Stobienia, O., Budzińska, M., and Kmita, H. 2001b. Under conditions of insufficient permeability of VDAC1 external NADH may use the TOM complex channel to cross the outer membrane of Saccharomyces cerevisiae mitochondria. J. Bioenerg. Biomembr. 33:119–126.
   PubMedGoogle Scholar
• Benz, R. 1994. Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins. Biochim. Biophys. Acta 1197:167–196.
   PubMed Web of Science ®Google Scholar
• Blachly-Dyson, E., and Forte, M. 2001. VDAC channels. IUBMB Life 52:113–118.
   PubMed Web of Science ®Google Scholar
• Blachly-Dyson, E., Song, J., Wolfgang, W. J., Colombini, M., and Forte, M. 1997. Multicopy supressors of phenotypes resulting from the absence of yeast VDAC-like protein. Mol. Cell Biol. 17:5727–5738.
   PubMed Web of Science ®Google Scholar
• Blachly-Dyson, E., Zambrowicz, E. B., Yu, W. H., Adams, V., McCabe, E. R. B., Adelman, J., and Colombini, M. 1993. Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel. J. Biol. Chem. 268:1835–1841
   PubMed Web of Science ®Google Scholar
• Braun, H. P., and Schmitz, U. K. 1999. The protein-import apparatus of plant mitochondria. Planta 209:267–274.
   PubMedGoogle Scholar
• Brdiczka, D. 1991. Contact sites between mitochondrial envelope membranes: structure and function in energy and protein transfer. Biochim. Biophys. Acta 1071:291–312.
   PubMedGoogle Scholar
• Colombini, M., Blachly-Dyson, E., and Forte M. 1996. VDAC, a channel in the outer mitochondrial membrane. In Ion Channels, ed. T. Narahashi, 169–201. New York: Plenum Press.
   Google Scholar
• Crompton, M., Barksby, E., Johnson, N., and Capano, M. 2002. Mitochondrial intermembrane junctional complexes and their involvement in cell death. Biochimie 84:143–152.
   PubMed Web of Science ®Google Scholar
• Dekker, P. J., Martin, F., Maarse, A. C., Bömer, U., Müller, H., Guiard, B., Meijer, M., Rassow, J., and Pfanner, N. 1997. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16:5408–5419.
   PubMed Web of Science ®Google Scholar
• De Vries, S., and Marres, C. A. 1987. The mitochondrial respiratory chain of yeast: structure and biosynthesis and the role in cellular metabolism. Biochim. Biophys. Acta 895:205–239.
   PubMedGoogle Scholar
• Dihanich, M., Suda, K., and Schatz., G. 1987. A yeast lacking mitochondrial porin is respiratory deficient, but can recover respiration with simultanous accumulation of an 86-kDa extramitochondrial protein. EMBO J. 6:723–728.
   PubMedGoogle Scholar
• Elkeles, A., Breiman, A., and Zizi, M. 1997. Functional differences among wheat voltage-dependent anion channel (VDAC) isoforms expressed in yeast. J. Biol. Chem. 272:6252–6260.
   Google Scholar
• Heins, L., Mentzel, H., Schmid, A., Benz, R., and Schmitz, U. K. 1994. Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria. J. Biol. Chem. 269:26402–26410.
   PubMedGoogle Scholar
• Hill, K., Model, K., Ryan, M. T., Dietmeier, K., Martin, F., Wagner, R., and Pfanner, N. 1998. Tom 40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395:516–521.
   PubMedGoogle Scholar
• Holden, M. J., and Colombini, M. 1988. The mitochondrial outer membrane channel, VDAC, is modulated byasolubleprotein. FEBS Lett. 241:105–109.
   PubMed Web of Science ®Google Scholar
• Holden, M. J., and Colombini, M. 1993. The outer mitochondrial membrane channel, VDAC, is modulated by a protein localized in the intermembrane space. Biochim. Biophys. Acta 1144:396–402.
   PubMedGoogle Scholar
• Kmita, H., and Budzińska, M. 2000. Involvement of the TOM complex in external NADH transport into yeast mitochondria depleted of mitochondrial porin. Biochim. Biophys. Acta 1509:86–94.
   PubMedGoogle Scholar
• Kmita, H., Budzińska, M., and Stobienia, O. 2003. Modulation of the voltage-dependent anion-selective channel by cytoplasmic proteins from wild type and the channel depleted cells of Saccharomyces cerevisiae. Acta Biochim. Pol. 50:415–424.
   PubMedGoogle Scholar
• Kmita, H., Stobienia, O., and Michejda, J. 1999. The access of metabolites into yeast mitochondria in the presence and absence of the voltage-dependent anion selective channel (YVDAC1). Acta Biochim. Pol. 46:991–1000.
   PubMedGoogle Scholar
• Künkele, K. P., Heins, S., Dembowski, M., Nargang, F. E., Benz, R., Thieffry, M., Walz, J., Lill, R., Nussberger, S., and Neupert, W. 1998a. The preprotein translocation channel of the outer membrane of mitochondria. Cell 93:1009–1019.
   PubMedGoogle Scholar
• Künkele, K. P., Juin, P., Pompa, C., Nargang, F. E., Henry, J.-P., Neupert, W., Lill, R., and Thieffry, M. 1998b. The isolated complex of the translocase of the outer membrane of mitochondria. J. Biol. Chem. 273:31032–31039.
   PubMedGoogle Scholar
• Lee, A. C., Xu, X., Blachly-Dyson, E., Forte, M., and Colombini M. 1998. The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane. J. Membr. Biol. 161:173–181.
   PubMedGoogle Scholar
• Lemeshko, V. V. 2002. Model of the outer membrane potential generation by the inner membrane of mitochondria. Biophys J. 82:684–692.
   PubMedGoogle Scholar
• Liu, M. Y., and Colombini, M. 1992. Regulation of mitochondrial respiration by controlling the permeability of the outer membrane through the mitochondrial channel, VDAC. Biochim. Biophys. Acta 1098:255–260.
   PubMed Web of Science ®Google Scholar
• Liu, M. Y, Torgrimson, A., and Colombini, M., 1994. Characterization and partial purification of the VDAC-channel–modulating protein from calf liver mitochondria. Biochim. Biophys. Acta 1185:203–212.
   PubMedGoogle Scholar
• Mannella, C. A. 1997. Minireview: on the structure and gating mechanism of the mitochondrial channel VDAC. J. Bioenerg. Biomembr. 49:525–531.
   Google Scholar
• Meisinger, C., Ryan, M. T., Hill, K., Model, K., Lim, J. H., Sickmann, A., Mueller, H., Meyer, H. E., Wagner, R., and Pfanner, N. 2001. Protein import channel of the outer mitochondrial membrane: a highly stable Tom40–Tom22 core structure differentially interacts with preproteins, small Tom proteins and import receptors. Mol. Cell Biol. 21:2337–2348.
   PubMed Web of Science ®Google Scholar
• Michejda, J., Guo, X. J., and Lauquin., C. J. M. 1990. Therespiration of cells and mitochondria of porin-deficient yeast mutants is coupled. Biochem. Biophys. Res. Commun. 171:354–361.
   PubMedGoogle Scholar
• Michejda, J., Kmita, H., Stobienia, O., Budzińska, M., and Lauquin, G. J. M. 1994. Restriction of metabolite permeation through the outer mitochondrial membrane of porin-deficient yeast mutant. In Molecular Biology of Mitochondrial Transport System, ed. M. Forte and M. Colombini, 341–356. Heidelberg, Germany: Springer-Verlag.
   Google Scholar
• Model, K., Prinz, T., Ruiz, T., Radermacher, M., Krimmer, T., Kühlbrandt, W., Pfanner, N., and Meisinger, C. 2002. Protein translocase of the outer mitochondrial membrane: role of receptors in the structural organization of the TOM complex. J. Miol. Biol. 316:657–666.
   PubMedGoogle Scholar
• Mori, M., and Terada, K. 1998. Mitochondrial protein import in animals. Biochim. Biophys. Acta 1403:12–27.
   PubMedGoogle Scholar
• Paschen, S.A., and Neupert, W. 2001. Protein import into mitochondria. IUBMB Life 52:101–112.
   PubMed Web of Science ®Google Scholar
• Pfanner, N., and Chacińska, A. 2002. The mitochondrial import machinery: preprotein-conducting channels with binding sites for presequences. Biochim. Biophys. Acta 1592:15–24.
   PubMedGoogle Scholar
• Prohl, C., Pelzer, W., Diekert, K., Kmita, H., Bedekovics, T., Kispal, G., and Lill, R. 2001. The yeast mitochondrial carrier Leu5p and its human homologue Graves’ disease protein are required for accumulation of coenzyme A in the matrix. Mol. Cell Biol. 21:1089–1097.
   PubMed Web of Science ®Google Scholar
• Rapaport, D. 2002. Biogenesis of the mitochondrial TOM complex. Trends Biochem. Sci. 27:191–197.
   PubMedGoogle Scholar
• Rapaport, D., Künkele, K. P., Dembowski, M., Ahting, U., Nargang, F. E., Neupert, W., and Lill, R. 1998a. Dynamics of the Tom complex of mitochondria during binding and translocation of preproteins. Mol. Cell Biol. 18:5256–5262.
   PubMedGoogle Scholar
• Rapaport, D., Mayer, A., Neupert, W, and Lill, R. 1998b. Cis and trans sites of the TOM complex of mitochondria in unfolding and initial translocation of preproteins. J. Biol. Chem. 273:8806–8813.
   PubMedGoogle Scholar
• Sampson, M. J., Lovell, R. S., and Craigen, W. J. 1997. The mouse VDAC gene family: conserved structure and function. J. Biol. Chem. 272:18966–18973.
   PubMedGoogle Scholar
• Shimizu, S., Ide, T., Yanagida, T., and Tsujimoto, Y. 2000. Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J. Biol. Chem. 275:12321–12325.
   PubMed Web of Science ®Google Scholar
• Sirrenberg, C., Endres, M., Becker, K., Bauer, M. F., Walther, E., Neupert, W., and Brunner, M. 1997. Functional cooperation and stechiometry of protein translocases of the outer and inner membranes of mitochondria. J. Biol. Chem. 272:29963–29966.
   PubMed Web of Science ®Google Scholar
• Stobienia, O., Wróblewska, S., Antos, N., Budzińska, M., and Kmita, H. 2002. The key role of the energized state of Saccharomyces cerevisiae mitochondria in modulations of the outer membrane channels by the intermembrane space proteins. J. Bioenerg. Biomembr. 34:507–516.
   PubMedGoogle Scholar
• Suzuki, H., Okazawa, Y., Komiya, T., Saeki, K., Mekada, E., Kitada, S., Ito, A., and Mihara, K. 2000. Characterization of rat Tom 40, a central component of the preprotein translocase of the mitochondrial outer membrane. J. Biol. Chem. 275:37930–37936.
   PubMedGoogle Scholar
• Tsujimoto, Y., and Shimizu, S. 2002. The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84:187–193.
   PubMed Web of Science ®Google Scholar
• Vander Heiden, M. G., Chandel, N. S., Li, X. X., Schumacker, P. T., Colombini, M., and Thompson, C. B. 2000. Outer mitochondrial membrane permeability can regulate coupled respiration and cell survival. Proc. Natl. Acad. Sci. U S A 97:4666–4671.
   PubMedGoogle Scholar
• van Wilpe, S., Ryan, M. T., Hill, K., Maarse, A. C., Meisinger, C., Brix, J., Dekker, P. J. T., Moczko, M., Wagner, R., Meijer, M., Guiard, B., Hönlinger, A., and Pfanner, N. 1999. Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase. Nature 401:485–489.
   PubMedGoogle Scholar
• Xu, X., Decker, W., Sampson, M. J., Craigen, W. J., and Colombini, M. 1999. Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability. J. Membr. Biol. 170:89–102.
   PubMedGoogle Scholar