메뉴 건너뛰기




Volumn 161, Issue 2, 1998, Pages 173-181

The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane

Author keywords

Dehydrogenase; Mitochondria; NADH; Outer membrane; VDAC

Indexed keywords

ANION CHANNEL; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 15644371838     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900324     Document Type: Article
Times cited : (145)

References (30)
  • 1
    • 0025796715 scopus 로고
    • Porin interaction with hexokinase and glycerol kinase: Metabolic microcompartmentation at the outer mitochondrial membrane
    • Adams, V., Griffin, L., Towbin, J., Gelb, B., Worley, K., McCabe, E.R.B. 1991. Porin interaction with hexokinase and glycerol kinase: metabolic microcompartmentation at the outer mitochondrial membrane. Biochem. Med. Metabol. Biol. 45:271-291
    • (1991) Biochem. Med. Metabol. Biol. , vol.45 , pp. 271-291
    • Adams, V.1    Griffin, L.2    Towbin, J.3    Gelb, B.4    Worley, K.5    McCabe, E.R.B.6
  • 2
    • 0024284216 scopus 로고
    • Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion
    • Benz, R., Wojtczak, L., Bosch, W., Brdiczka, D. 1988. Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion. FEBS Lett. 231:75-80
    • (1988) FEBS Lett. , vol.231 , pp. 75-80
    • Benz, R.1    Wojtczak, L.2    Bosch, W.3    Brdiczka, D.4
  • 3
    • 0025355620 scopus 로고
    • Selectivity changes in site-directed mutants of the VDAC ion channel: Structural implications
    • Blachly-Dyson, E., Peng, S.Z., Colombini, M., Forte, M. 1990. Selectivity changes in site-directed mutants of the VDAC ion channel: structural implications. Science 247:1233-1236
    • (1990) Science , vol.247 , pp. 1233-1236
    • Blachly-Dyson, E.1    Peng, S.Z.2    Colombini, M.3    Forte, M.4
  • 4
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson, E., Song, J., Wolfgang, W.J., Colombini, M., Forte, M. 1997. Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein. Molec. Cell. Biol. 17:5727-5738
    • (1997) Molec. Cell. Biol. , vol.17 , pp. 5727-5738
    • Blachly-Dyson, E.1    Song, J.2    Wolfgang, W.J.3    Colombini, M.4    Forte, M.5
  • 5
    • 0027389308 scopus 로고
    • Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel
    • Blachly-Dyson, E., Zambrowicz, E.B., Yu, W.H., Adams, V., McCabe, E.R.B., Adelman, J., Colombini, M., Forte, 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
    • (1993) J. Biol. Chem. , vol.268 , pp. 1835-1841
    • Blachly-Dyson, E.1    Zambrowicz, E.B.2    Yu, W.H.3    Adams, V.4    McCabe, E.R.B.5    Adelman, J.6    Colombini, M.7    Forte, M.8
  • 6
    • 0018775962 scopus 로고
    • A candidate for the permeability pathway of the outer mitochondrial membrane
    • Colombini, M. 1979. A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 279:643-645
    • (1979) Nature , vol.279 , pp. 643-645
    • Colombini, M.1
  • 7
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • T. Narahashi, editor, Plenum, New York
    • Colombini, M., Blachly-Dyson, E., Forte, M. 1996. VDAC, a channel in the outer mitochondrial membrane. In: Ion Channels Vol. 4. T. Narahashi, editor, pp. 169-202. Plenum, New York
    • (1996) Ion Channels , vol.4 , pp. 169-202
    • Colombini, M.1    Blachly-Dyson, E.2    Forte, M.3
  • 8
    • 0023513271 scopus 로고
    • The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion
    • Colombini, M., Yeung, C.L., Tung, J., König, T. 1987. The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion. Biochem. Biophys. Acta 905:279-286
    • (1987) Biochem. Biophys. Acta , vol.905 , pp. 279-286
    • Colombini, M.1    Yeung, C.L.2    Tung, J.3    König, T.4
  • 9
    • 0020479807 scopus 로고
    • 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257:13028-13033
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.C.2    Schatz, G.3
  • 10
    • 0023303620 scopus 로고
    • A yeast mutant lacking mitochondrial porin is respiratory-deficient, but can recover respiration with simultaneous accumulation of an 86-kd extramitochondrial protein
    • Dihanich, M., Suda, K., Schatz, G. 1987. A yeast mutant lacking mitochondrial porin is respiratory-deficient, but can recover respiration with simultaneous accumulation of an 86-kd extramitochondrial protein. EMBO J. 6:723-728
    • (1987) EMBO J. , vol.6 , pp. 723-728
    • Dihanich, M.1    Suda, K.2    Schatz, G.3
  • 11
    • 77957088304 scopus 로고
    • Isolation of plant mitochondria: General principles and criteria of integrity
    • Douce, R., Bourguignon, J., Brouquisse, R., Neuburger, M. 1987. Isolation of plant mitochondria: general principles and criteria of integrity. Methods Enzymol. 148:403-412
    • (1987) Methods Enzymol. , vol.148 , pp. 403-412
    • Douce, R.1    Bourguignon, J.2    Brouquisse, R.3    Neuburger, M.4
  • 12
    • 0015928859 scopus 로고
    • The external NADH dehydrogenases of intact plant mitochondria
    • Douce, R., Mannella, C.A., Bonner, W.D. 1973. The external NADH dehydrogenases of intact plant mitochondria. Biochim. Biophys. Acta 292:105-116
    • (1973) Biochim. Biophys. Acta , vol.292 , pp. 105-116
    • Douce, R.1    Mannella, C.A.2    Bonner, W.D.3
  • 13
    • 0025212128 scopus 로고
    • Comparison of mitochondrial cationic channels in wild-type and porin-deficient mutant yeast
    • Fevre, F., Chich, J.F., Lauquin, G.J., Henry, J.P., Thieffry, M. 1990. Comparison of mitochondrial cationic channels in wild-type and porin-deficient mutant yeast. FEBS Lett. 262:201-4
    • (1990) FEBS Lett. , vol.262 , pp. 201-204
    • Fevre, F.1    Chich, J.F.2    Lauquin, G.J.3    Henry, J.P.4    Thieffry, M.5
  • 14
    • 0029683049 scopus 로고    scopus 로고
    • Structure and function of the yeast outer mitochondrial membrane channel, VDAC
    • Forte, M., Blachly-Dyson, E., Colombini, M. 1996. Structure and function of the yeast outer mitochondrial membrane channel, VDAC. J. Gen. Physiol. 51:145-154
    • (1996) J. Gen. Physiol. , vol.51 , pp. 145-154
    • Forte, M.1    Blachly-Dyson, E.2    Colombini, M.3
  • 15
    • 0027166976 scopus 로고
    • Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate kinase in the inter-membrane space
    • Gellerich, F.N., Wagner, M., Kapischke, M., Wicker, U., Brdiczka, D. 1993. Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate kinase in the inter-membrane space. Biochim. Biophys. Acta 1142:217-227
    • (1993) Biochim. Biophys. Acta , vol.1142 , pp. 217-227
    • Gellerich, F.N.1    Wagner, M.2    Kapischke, M.3    Wicker, U.4    Brdiczka, D.5
  • 16
    • 0000614252 scopus 로고
    • Uncoupling of oxidative phosphorylation by Carbonyl Cyanide Phenylhydrazones. I. Some characteristics of m-Cl-CCP action of mitochondria and chloroplasts
    • Heytler, P.G. 1963. Uncoupling of oxidative phosphorylation by Carbonyl Cyanide Phenylhydrazones. I. Some characteristics of m-Cl-CCP action of mitochondria and chloroplasts. Biochemistry 2:357-361
    • (1963) Biochemistry , vol.2 , pp. 357-361
    • Heytler, P.G.1
  • 17
    • 0024279569 scopus 로고
    • The mitochondrial outer membrane channel. VDAC, is modulated by a soluble protein
    • Holden, M.J., Colombini, M. 1988. The mitochondrial outer membrane channel. VDAC, is modulated by a soluble protein. FEBS Lett. 241:105-109
    • (1988) FEBS Lett. , vol.241 , pp. 105-109
    • Holden, M.J.1    Colombini, M.2
  • 18
    • 0015948722 scopus 로고
    • Mechanisms of active transport in isolated bacterial membrane vesicles XVIII. The mechanism of action of Carbonylcyanide m-Chlorophenylhydrazone
    • Kaback, H.R., Reeves, J.P., Short, S.A., Lombardi, F.J. 1974. Mechanisms of active transport in isolated bacterial membrane vesicles XVIII. The mechanism of action of Carbonylcyanide m-Chlorophenylhydrazone. Arch. Biochem. Biophys. 160:215-222
    • (1974) Arch. Biochem. Biophys. , vol.160 , pp. 215-222
    • Kaback, H.R.1    Reeves, J.P.2    Short, S.A.3    Lombardi, F.J.4
  • 19
    • 0028172237 scopus 로고
    • β-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6
    • Lee, A., Zizi, M., Colombini, M. 1994. β-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6. J. Biol. Chem. 269:30974-30980
    • (1994) J. Biol. Chem. , vol.269 , pp. 30974-30980
    • Lee, A.1    Zizi, M.2    Colombini, M.3
  • 20
    • 0030050144 scopus 로고    scopus 로고
    • Identification of porin as binding site for MAP2
    • Linden, M. and Karlsson, G. 1996. Identification of porin as binding site for MAP2. Biochem. Biophys. Res. Commun. 218:833-6
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 833-836
    • Linden, M.1    Karlsson, G.2
  • 21
    • 0026542990 scopus 로고
    • Regulation of mitochondrial respiration by controlling the permeability of the outer membrane through the mitochondrial channel. VDAC
    • Liu, M., 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
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 255-260
    • Liu, M.1    Colombini, M.2
  • 22
    • 0021770701 scopus 로고
    • Evidence that the crystalline arrays in the outer membrane of Neurospora mitochondria are composed of the voltage-dependent channel protein
    • Mannella, C.A., Colombini, M. 1984. Evidence that the crystalline arrays in the outer membrane of Neurospora mitochondria are composed of the voltage-dependent channel protein. Biochim. Biophys. Acta 774:206-214
    • (1984) Biochim. Biophys. Acta , vol.774 , pp. 206-214
    • Mannella, C.A.1    Colombini, M.2
  • 23
    • 0026538575 scopus 로고
    • Toward the molecular structure of the mitochondrial channel. VDAC
    • Mannella, C.A., Forte, M., Colombini, M. 1992. Toward the molecular structure of the mitochondrial channel. VDAC. J. Bioenerg. Biomembr. 24:7-19
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 7-19
    • Mannella, C.A.1    Forte, M.2    Colombini, M.3
  • 24
    • 0025166965 scopus 로고
    • The respiration of cells and mitochondria of porin deficient yeast mutants is coupled
    • Michejda, J., Guo, X.J., Lauquin, G.J.-M. 1990. The respiration of cells and mitochondria of porin deficient yeast mutants is coupled. Biochem. Biophys. Res. Commun. 171:354-361
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 354-361
    • Michejda, J.1    Guo, X.J.2    Lauquin, G.J.-M.3
  • 25
    • 0242587873 scopus 로고
    • 2+ in the oxidation of exogenous NADH by Jerusalem-artichoke (Helianthus tuberosus) mitochondria
    • 2+ in the oxidation of exogenous NADH by Jerusalem-artichoke (Helianthus tuberosus) mitochondria. Biochem. J. 194:487-495
    • (1981) Biochem. J. , vol.194 , pp. 487-495
    • Møller, I.M.1    Johnston, S.P.2    Palmer, J.M.3
  • 26
    • 0014027335 scopus 로고
    • Preparation and some properties of yeast mitochondria
    • Ohnishi, T., Kawaguchi, K., Hagihara, B. 1966. Preparation and some properties of yeast mitochondria. J. Biol. Chem. 241:1797-1806
    • (1966) J. Biol. Chem. , vol.241 , pp. 1797-1806
    • Ohnishi, T.1    Kawaguchi, K.2    Hagihara, B.3
  • 27
    • 0001525440 scopus 로고
    • An enzymatic approach to the study of the Krebs tricarboxylic acid cycle
    • V.M. Darley-Usmar, D. Rickwood and M.T. Wilson, editors. IRL Press, Washington, D.C.
    • Robinson, J.B., Brent, L.G., Sumegi, B., Srere, P.A. 1987. An enzymatic approach to the study of the Krebs tricarboxylic acid cycle. In: Mitochondria a Practical Approach. V.M. Darley-Usmar, D. Rickwood and M.T. Wilson, editors. pp. 153-170. IRL Press, Washington, D.C.
    • (1987) Mitochondria a Practical Approach , pp. 153-170
    • Robinson, J.B.1    Brent, L.G.2    Sumegi, B.3    Srere, P.A.4
  • 28
    • 0015862934 scopus 로고
    • The concentrations of free and bound Magnesium in rat tissues
    • Veloso, D., Guynn, R.W., Oskarsson, M., Veech, R.L. 1973. The concentrations of free and bound Magnesium in rat tissues. J. Biol. Chem. 248:4811-4819
    • (1973) J. Biol. Chem. , vol.248 , pp. 4811-4819
    • Veloso, D.1    Guynn, R.W.2    Oskarsson, M.3    Veech, R.L.4
  • 29
    • 0023041574 scopus 로고
    • Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel
    • Zimmerberg, J., Parsegian, V.A. 1986. Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel. Nature 323:36-39
    • (1986) Nature , vol.323 , pp. 36-39
    • Zimmerberg, J.1    Parsegian, V.A.2
  • 30
    • 0028158479 scopus 로고
    • NADH regulates the gating of VDAC, the mitochondrial outer membrane channel
    • Zizi, M., Forte, M., Blachly-Dyson, E., Colombini, M. 1994. NADH regulates the gating of VDAC, the mitochondrial outer membrane channel. J. Biol. Chem. 269:1614-1616
    • (1994) J. Biol. Chem. , vol.269 , pp. 1614-1616
    • Zizi, M.1    Forte, M.2    Blachly-Dyson, E.3    Colombini, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.