메뉴 건너뛰기




Volumn 72, Issue 5, 1997, Pages 1954-1962

Vdac channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0030947935     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78841-6     Document Type: Article
Times cited : (308)

References (40)
  • 1
    • 0027534155 scopus 로고
    • Transport properties and inhibitor sensitivity of isolated and reconstituted porin differ from those of intact mitochondria
    • Báthori, G., M. Sahin-Tóth, A. Fonyó, and E. Ligeti. 1993. Transport properties and inhibitor sensitivity of isolated and reconstituted porin differ from those of intact mitochondria. Biochim. Biophys. Acta. 1145: 168-176.
    • (1993) Biochim. Biophys. Acta , vol.1145 , pp. 168-176
    • Báthori, G.1    Sahin-Tóth, M.2    Fonyó, A.3    Ligeti, E.4
  • 2
    • 0026574501 scopus 로고
    • The cation-selective substrate of the mitochondrial outer membrane pore: Single-channel conductance and influence on intermembrane and peripheral kinases
    • Benz, R., and D. Brdiczka. 1992. The cation-selective substrate of the mitochondrial outer membrane pore: single-channel conductance and influence on intermembrane and peripheral kinases. J. Bioenerg. Biomembr. 24:33-39.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 33-39
    • Benz, R.1    Brdiczka, D.2
  • 3
    • 0025055329 scopus 로고
    • The cationically selective state of the mitochondrial outer membrane pore: A study with intact mitochondria and reconstituted mitochondrial porin
    • Benz, R., M. Catch, and D. Brdiczka. 1990. The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin. Biochim. Biophys. Acta. 1022:311-318.
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 311-318
    • Benz, R.1    Catch, M.2    Brdiczka, D.3
  • 4
    • 0024284216 scopus 로고
    • Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion
    • Benz, R., L. Wojtczak, W. Bosch, and D. Brdiczka. 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
  • 5
    • 0028465092 scopus 로고
    • Counting polymers moving through a single ion channel
    • Bezrukov, S. M., I. Vodyanoy, and V. A. Parsegian. 1994. Counting polymers moving through a single ion channel. Nature. 370:279-281.
    • (1994) Nature , vol.370 , pp. 279-281
    • Bezrukov, S.M.1    Vodyanoy, I.2    Parsegian, V.A.3
  • 6
    • 0025355620 scopus 로고
    • Selectivity changes in site-directed mutants of the VDAC ion channel: Structural implications
    • Blachly-Dyson, E., S. Peng, M. Colombini, and M. Forte. 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.2    Colombini, M.3    Forte, M.4
  • 7
    • 0028034636 scopus 로고
    • In vitro complex formation between the octamer of mitochondrial creatine kinase and porin
    • Brdiczka, D., P. Kaldis, and T. Wallimann. 1994. In vitro complex formation between the octamer of mitochondrial creatine kinase and porin. J. Biol. Chem. 269:27640-27644.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 8
    • 0000336786 scopus 로고
    • The effects of 2,4-dinitrophenol on mitochondrial oxidations
    • Chappell, J. B. 1964. The effects of 2,4-dinitrophenol on mitochondrial oxidations. Biochem. J. 90:237-248.
    • (1964) Biochem. J. , vol.90 , pp. 237-248
    • Chappell, J.B.1
  • 9
    • 0018847077 scopus 로고
    • Structure and mode of action of a voltage-dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane
    • Colombini, M. 1980. Structure and mode of action of a voltage-dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane. Ann. N.Y. Acad. Sci. 341:552-563.
    • (1980) Ann. N.Y. Acad. Sci. , vol.341 , pp. 552-563
    • Colombini, M.1
  • 10
    • 0024458675 scopus 로고
    • Voltage gating in the mitochondrial channel, VDAC
    • Colombini, M. 1989. Voltage gating in the mitochondrial channel, VDAC. J. Membr. Biol. 111:103-111.
    • (1989) J. Membr. Biol. , vol.111 , pp. 103-111
    • Colombini, M.1
  • 11
    • 79959414421 scopus 로고
    • Anion channels in the mitochondrial outer membrane
    • W. Guggino, editor. Academic Press, San Diego, CA
    • Colombini, M. 1994. Anion channels in the mitochondrial outer membrane. In Current Topics in Membranes, Vol. 42. W. Guggino, editor. Academic Press, San Diego, CA. 73-101.
    • (1994) Current Topics in Membranes , vol.42 , pp. 73-101
    • Colombini, M.1
  • 12
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • T. Narahashi, editor. Plenum Press, New York
    • Colombini, M., E. Blachy-Dyson, and M. Forte. 1996. VDAC, a channel in the outer mitochondrial membrane. In Ion Channels, Vol. 4. T. Narahashi, editor. Plenum Press, New York. 169-202.
    • (1996) Ion Channels , vol.4 , pp. 169-202
    • Colombini, M.1    Blachy-Dyson, E.2    Forte, M.3
  • 13
    • 0023513271 scopus 로고
    • The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion
    • Colombini, M., C. L. Yeung, J. Tung, and T. König. 1987. The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion. Biochim. Biophys. Acta. 905:279-286.
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 279-286
    • Colombini, M.1    Yeung, C.L.2    Tung, J.3    König, T.4
  • 14
    • 0013636810 scopus 로고
    • Springer-Verlag, Berlin
    • Diehl, H., H. Ihlefeld, and H. Schwegler. 1991. Physik für biologen. Springer-Verlag, Berlin. 391. (also available at WWW site: http:// www.df.unibo.it:8000/ishtar/html/diffu/tabelle_low.html)
    • (1991) Physik für Biologen , pp. 391
    • Diehl, H.1    Ihlefeld, H.2    Schwegler, H.3
  • 15
    • 0024277423 scopus 로고
    • Activation of mitochondrial oxidative metabolism by calcium ions in Limulus ventral photoreceptor
    • Fein, A., and M. Tsacopoulos. 1988. Activation of mitochondrial oxidative metabolism by calcium ions in Limulus ventral photoreceptor. Nature. 331:437-440.
    • (1988) Nature , vol.331 , pp. 437-440
    • Fein, A.1    Tsacopoulos, M.2
  • 17
    • 0020995433 scopus 로고
    • Isolation and properties of the porin of the outer mitochondrial membrane from Neurospora crassa
    • Freitag, H., R. Benz, and W. Neupert. 1983. Isolation and properties of the porin of the outer mitochondrial membrane from Neurospora crassa. Methods Enzymol. 97:286-294.
    • (1983) Methods Enzymol. , vol.97 , pp. 286-294
    • Freitag, H.1    Benz, R.2    Neupert, W.3
  • 18
    • 0027166976 scopus 로고
    • Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate kinase in the intermembrane space
    • Gellerich, F. N., M. Wagner, M. Kapischke, U. Wicker, and D. Brdiczka. 1993. Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate kinase in the intermembrane 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
  • 19
    • 0029143569 scopus 로고
    • Decoding of cytosolic calcium oscillations in the mitochondria
    • Hajnoczky, G., L. D. Robb-Gaspers, M. B. Scitz, and A. P. Thomas. 1995. Decoding of cytosolic calcium oscillations in the mitochondria. Cell. 82:415-424.
    • (1995) Cell , vol.82 , pp. 415-424
    • Hajnoczky, G.1    Robb-Gaspers, L.D.2    Scitz, M.B.3    Thomas, A.P.4
  • 20
    • 0030958679 scopus 로고    scopus 로고
    • Regulation of metabolite flux through voltage-gating of VDAC channels
    • in press
    • Hodge, T., and M. Colombini. 1997. Regulation of metabolite flux through voltage-gating of VDAC channels. J. Membr. Biol. 157:(in press).
    • (1997) J. Membr. Biol. , vol.157
    • Hodge, T.1    Colombini, M.2
  • 21
    • 0024279569 scopus 로고
    • The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein
    • Holden, M. J., and M. Colombini. 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
  • 22
    • 0027527234 scopus 로고
    • The outer mitochondrial membrane channel, VDAC, is modulated by a protein localized in the intermembrane space
    • Holden, M. J., and M. Colombini. 1993. The outer mitochondrial membrane channel, VDAC, is modulated by a protein localized in the intermembrane space. Biochim. Biophys. Acta. 1144:396-402.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 396-402
    • Holden, M.J.1    Colombini, M.2
  • 23
    • 0028172237 scopus 로고
    • β-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6
    • Lee, A.-C., M. Zizi, and M. Colombini. 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.-C.1    Zizi, M.2    Colombini, M.3
  • 25
    • 0026542990 scopus 로고
    • Regulation of mitochondrial respiration by controlling the permeability of the outer membrane through the mitochondrial channel, VDAC
    • Liu, M. Y., and M. Colombini. 1992a. 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.Y.1    Colombini, M.2
  • 26
    • 0026507895 scopus 로고
    • A soluble protein increases the voltage dependence of the mitochondrial channel, VDAC
    • Liu, M. Y., and M. Colombini. 1992b. A soluble protein increases the voltage dependence of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 24:41-46.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 41-46
    • Liu, M.Y.1    Colombini, M.2
  • 27
    • 0023373137 scopus 로고
    • Ultrasteep voltage dependence in a membrane channel
    • Mangan, P., and M. Colombini. 1987. Ultrasteep voltage dependence in a membrane channel. Proc. Natl. Acad. Sci. USA. 84:4896-4900.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4896-4900
    • Mangan, P.1    Colombini, M.2
  • 28
    • 0020450839 scopus 로고
    • Structure of the outer mitochondrial membrane: Ordered arrays of pore-like subunits in outer-membrane fractions from Neurospora crassa mitochondria
    • Mannella, C. 1982. Structure of the outer mitochondrial membrane: ordered arrays of pore-like subunits in outer-membrane fractions from Neurospora crassa mitochondria. J. Cell Biol. 94:680-687.
    • (1982) J. Cell Biol. , vol.94 , pp. 680-687
    • Mannella, C.1
  • 29
    • 0025191408 scopus 로고
    • Interaction between the VDAC channel and a polyanionic effector
    • Mannella, C. A., and X. W. Guo. 1990. Interaction between the VDAC channel and a polyanionic effector. Biophys. J. 57:23-31.
    • (1990) Biophys. J. , vol.57 , pp. 23-31
    • Mannella, C.A.1    Guo, X.W.2
  • 30
    • 0015459562 scopus 로고
    • Formation of biomolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal, M., and P. Mueller. 1972. Formation of biomolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA. 69:3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 31
    • 0026696184 scopus 로고
    • Large scale rearrangement of protein domains is associated with voltage gating of the VDAC channel
    • Peng, S., E. Blachly-Dyson, M. Forte, and M. Colombini. 1992. Large scale rearrangement of protein domains is associated with voltage gating of the VDAC channel. Biophys. J. 62:123-135.
    • (1992) Biophys. J. , vol.62 , pp. 123-135
    • Peng, S.1    Blachly-Dyson, E.2    Forte, M.3    Colombini, M.4
  • 32
    • 0029854155 scopus 로고    scopus 로고
    • ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane
    • Rostovtseva, T., and M. Colombini. 1996. ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane. J. Biol. Chem. 271:28006-28008.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28006-28008
    • Rostovtseva, T.1    Colombini, M.2
  • 33
    • 0017054558 scopus 로고
    • Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from Paramecium mitochondria
    • Schein, S. J., M. Colombini, and A. Finkelstein. 1976. Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from Paramecium mitochondria. J. Membr. Biol. 30: 99-120.
    • (1976) J. Membr. Biol. , vol.30 , pp. 99-120
    • Schein, S.J.1    Colombini, M.2    Finkelstein, A.3
  • 34
    • 0028865759 scopus 로고
    • Mitochondrial calcium uptake from physiological-type pulses of calcium. A description of the rapid uptake mode
    • Sparagna, G. C., K. K. Gunter, S. S. Sheu, and T. E. Gunter. 1995. Mitochondrial calcium uptake from physiological-type pulses of calcium. A description of the rapid uptake mode. J. Biol. Chem 270: 27510-27515.
    • (1995) J. Biol. Chem , vol.270 , pp. 27510-27515
    • Sparagna, G.C.1    Gunter, K.K.2    Sheu, S.S.3    Gunter, T.E.4
  • 35
    • 0027315863 scopus 로고
    • Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel
    • Thomas, L., E. Blachly-Dyson, M. Colombini, and M. Forte. 1993. Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel. Proc. Natl. Acad. Sci. USA. 90: 5446-5449.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5446-5449
    • Thomas, L.1    Blachly-Dyson, E.2    Colombini, M.3    Forte, M.4
  • 37
    • 0027293087 scopus 로고
    • Zero-current potentials in a large membrane channel: A simple theory accounts for complex behavior
    • Zambrowicz, E. B., and M. Colombini. 1993. Zero-current potentials in a large membrane channel: a simple theory accounts for complex behavior. Biophys. J. 65:1093-1100.
    • (1993) Biophys. J. , vol.65 , pp. 1093-1100
    • Zambrowicz, E.B.1    Colombini, M.2
  • 38
    • 0025715214 scopus 로고
    • Group IIIA-metal hydroxides indirectly neutralize the voltage sensor of the voltage-dependent mitochondrial channel, VDAC, by interacting with a dynamic binding site
    • Zhang, D.-W., and M. Colombini. 1990. Group IIIA-metal hydroxides indirectly neutralize the voltage sensor of the voltage-dependent mitochondrial channel, VDAC, by interacting with a dynamic binding site. Biochim. Biophys. Acta. 1025:127-134.
    • (1990) Biochim. Biophys. Acta , vol.1025 , pp. 127-134
    • Zhang, D.-W.1    Colombini, M.2
  • 39
    • 0023041574 scopus 로고
    • Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel
    • Zimmerberg, J., and V. A. Parsegian. 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
  • 40
    • 0028158479 scopus 로고
    • NADH regulates the gating of VDAC, the mitochondrial outer membrane channel
    • Zizi, M., M. Forte, E. Blachly-Dyson, and M. Colombini. 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.