메뉴 건너뛰기




Volumn 50, Issue 2, 2003, Pages 415-424

Modulation of the voltage-dependent anion-selective channel by cytoplasmic proteins from wild type and the channel depleted cells of Saccharomyces cerevisiae

Author keywords

Mitochondria; Reconstituted system; Saccharomyces cerevisiae; VDAC depleted mutant; Voltage dependent anion selective channel (VDAC); Yeast

Indexed keywords

CYTOPLASM PROTEIN;

EID: 0042882618     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2003_3695     Document Type: Article
Times cited : (11)

References (35)
  • 1
    • 0035968078 scopus 로고    scopus 로고
    • An interplay between the TOM complex and porin isoforms in the yeast Saccharomyces cerevisiae mitochondria
    • Antos N, Budzinska M, Kmita, H. (2001) An interplay between the TOM complex and porin isoforms in the yeast Saccharomyces cerevisiae mitochondria. FEBS Lett.; 500: 12-6.
    • (2001) FEBS Lett , vol.500 , pp. 12-16
    • Antos, N.1    Budzinska, M.2    Kmita, H.3
  • 2
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins
    • Benz R. (1994) Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins. Biochim Biophys Acta.; 1197: 167-96.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 3
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • Benz R, Janko K, Boos W, Lauger P. (1978) Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta.; 511: 305-19.
    • (1978) Biochim Biophys Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Lauger, P.4
  • 5
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotype resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson E, Song J, Wolfgang WJ, Colombini M, Forte M. (1997) Multicopy suppressors of phenotype resulting from the absence of yeast VDAC encode a VDAC-like protein. Mol Cell Biol.; 17: 5727-38.
    • (1997) Mol Cell Biol , vol.17 , pp. 5727-5738
    • Blachly-Dyson, E.1    Song, J.2    Wolfgang, W.J.3    Colombini, M.4    Forte, M.5
  • 6
    • 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 EB, Yu WH, Adams V, McCabe ERB, 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: 1835-41.
    • (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
  • 7
    • 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: 643-5.
    • (1979) Nature , vol.279 , pp. 643-645
    • Colombini, M.1
  • 8
    • 79959414421 scopus 로고
    • Anion channels in the mitochondrial outer membrane
    • Colombini M. (1994) Anion channels in the mitochondrial outer membrane. Curr Top Membr.; 42: 73-101.
    • (1994) Curr Top Membr , vol.42 , pp. 73-101
    • Colombini, M.1
  • 9
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • Narahashi T. ed. Plenum Press, New York
    • Colombini M, Blachly-Dyson E, Forte, M. (1996) VDAC, a channel in the outer mitochondrial membrane. In Ion Channels. Narahashi T. ed, pp 169-201. Plenum Press, New York.
    • (1996) Ion Channels , pp. 169-201
    • Colombini, M.1    Blachly-Dyson, E.2    Forte, M.3
  • 10
    • 0036479049 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their involvement in cell death
    • Crompton M, Barksby E, Johnson N, Capano M. (2002) Mitochondrial intermembrane junctional complexes and their involvement in cell death. Biochimie; 84: 143-52.
    • (2002) Biochimie , vol.84 , pp. 143-152
    • Crompton, M.1    Barksby, E.2    Johnson, N.3    Capano, M.4
  • 11
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum G, Bohni PC, Schatz G. (1982). Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J Biol Chem.; 257: 13028-33.
    • (1982) J Biol Chem , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 12
    • 0023659763 scopus 로고
    • Porin pores of mitochondrial outer membranes from high and low eukaryotic cells: Biochemical and biophysical characterization
    • De Pinto V, Ludwig O, Krause J, Benz R, Palmieri F. (1987) Porin pores of mitochondrial outer membranes from high and low eukaryotic cells: biochemical and biophysical characterization. Biochim Biophys Acta.; 894: 109-19.
    • (1987) Biochim Biophys Acta , vol.894 , pp. 109-119
    • De Pinto, V.1    Ludwig, O.2    Krause, J.3    Benz, R.4    Palmieri, F.5
  • 13
    • 0023561970 scopus 로고
    • The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism
    • De Vries S, Marres CA. (1987) The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim Biophys Acta.; 895: 205-39.
    • (1987) Biochim Biophys Acta , vol.895 , pp. 205-239
    • De Vries, S.1    Marres, C.A.2
  • 14
    • 77957088304 scopus 로고
    • Isolation of plant mitochondria. General principles and criteria of integrity
    • Douce R, Bourguignon R, Neuberger M. (1984) Isolation of plant mitochondria. General principles and criteria of integrity. Methods Enzymol.; 148: 403-15.
    • (1984) Methods Enzymol , vol.148 , pp. 403-415
    • Douce, R.1    Bourguignon, R.2    Neuberger, M.3
  • 15
    • 0030942846 scopus 로고    scopus 로고
    • Functional differences among wheat voltage-dependent anion channel (VDAC) isoforms expressed in yeast. Indication for the presence of a novel VDAC-modulating protein?
    • Elkeles A, Breiman A, Zizi M. (1997) Functional differences among wheat voltage-dependent anion channel (VDAC) isoforms expressed in yeast. Indication for the presence of a novel VDAC-modulating protein? J Biol Chem.; 272: 6252-60.
    • (1997) J Biol Chem , vol.272 , pp. 6252-6260
    • Elkeles, A.1    Breiman, A.2    Zizi, M.3
  • 16
    • 0028079979 scopus 로고
    • Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria
    • Heins L, Mentzel H, Schmid A, Benz R, Schmitz UK. (1994) Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria. J Biol Chem.; 269: 26402-10.
    • (1994) J Biol Chem , vol.269 , pp. 26402-26410
    • Heins, L.1    Mentzel, H.2    Schmid, A.3    Benz, R.4    Schmitz, U.K.5
  • 17
    • 0024279569 scopus 로고
    • The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein
    • Holden MJ, Colombini M. (1988) The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein. FEBS Lett.; 241: 105-9.
    • (1988) FEBS Lett , vol.241 , pp. 105-109
    • Holden, M.J.1    Colombini, M.2
  • 18
    • 0027527234 scopus 로고
    • The outer mitochondrial membrane channel, VDAC, is modulated by a protein localized in the intermembrane space
    • Holden MJ, 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.
    • (1993) Biochim Biophys Acta , vol.1144 , pp. 396-402
    • Holden, M.J.1    Colombini, M.2
  • 19
    • 0018665167 scopus 로고
    • Membrane potential of mitochondria measured with electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state
    • Kamo N, Muratsugu M, Hongoh R, Kobatake YJ (1979) Membrane potential of mitochondria measured with electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state. J Membr Biol.; 49: 105-21.
    • (1979) J Membr Biol , vol.49 , pp. 105-121
    • Kamo, N.1    Muratsugu, M.2    Hongoh, R.3    Kobatake, Y.J.4
  • 20
    • 0034695130 scopus 로고    scopus 로고
    • Involvement of the TOM complex in external NADH transport into yeast mitochondria depleted of mitochondrial porin1
    • Kmita H, Budzińska M. (2000) Involvement of the TOM complex in external NADH transport into yeast mitochondria depleted of mitochondrial porin1. Biochim Biophys Acta.; 1509: 86-94.
    • (2000) Biochim Biophys Acta , vol.1509 , pp. 86-94
    • Kmita, H.1    Budzińska, M.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 15644371838 scopus 로고    scopus 로고
    • The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane
    • Lee AC, Xu X, Blachly-Dyson E, Forte M, Colombini M. (1998) The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane. J Membr Biol.; 161: 173-81.
    • (1998) J Membr Biol , vol.161 , pp. 173-181
    • Lee, A.C.1    Xu, X.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 23
    • 0036151794 scopus 로고    scopus 로고
    • Model of the outer membrane potential generation by the inner membrane of mitochondria
    • Lemeshko VV. (2002) Model of the outer membrane potential generation by the inner membrane of mitochondria. Biophys J.; 82: 684-92.
    • (2002) Biophys J , vol.82 , pp. 684-692
    • Lemeshko, V.V.1
  • 24
    • 0025975055 scopus 로고
    • Voltage gating of the mitochondrial outer membrane channel VDAC is regulated by a very conserved protein
    • Liu MY, Colombini M. (1991) Voltage gating of the mitochondrial outer membrane channel VDAC is regulated by a very conserved protein. Am J Physiol.; 260: C371-4.
    • (1991) Am J Physiol , vol.260
    • Liu, M.Y.1    Colombini, M.2
  • 25
    • 0026542990 scopus 로고
    • Regulation of mitochondrial respiration by controlling the permeability of the outer membrane through the mitochondrial channel, VDAC
    • Liu MY, Colombini M. (1992) Regulation of mitochondrial respiration by controlling the permeability of the outer membrane through the mitochondrial channel, VDAC. Biochim Biophys Acta.; 1098: 255-60.
    • (1992) Biochim Biophys Acta , vol.1098 , pp. 255-260
    • Liu, M.Y.1    Colombini, M.2
  • 26
    • 0028348792 scopus 로고
    • Characterization and partial purification of the VDAC-channel-modulating protein from calf liver mitochondria
    • Liu MY, Torgrimson A, Colombini M. (1994) Characterization and partial purification of the VDAC-channel-modulating protein from calf liver mitochondria. Biochim Biophys Acta.; 1185: 203-12.
    • (1994) Biochim Biophys Acta , vol.1185 , pp. 203-212
    • Liu, M.Y.1    Torgrimson, A.2    Colombini, M.3
  • 27
    • 0000508699 scopus 로고
    • Restriction of metabolite permeation through the outer mitochondrial membrane of porin-deficient yeast mutant
    • Forte M, Colombini M. eds. Springer-Verlag, Heidelberg
    • Michejda J, Kmita H, Stobienia O, Budzińska M, Lauquin GJ-M. (1994) Restriction of metabolite permeation through the outer mitochondrial membrane of porin-deficient yeast mutant. In: molecular biology of mitochondrial transport system. Forte M, Colombini M. eds, pp 341-56. Springer-Verlag, Heidelberg.
    • (1994) Molecular Biology of Mitochondrial Transport System , pp. 341-356
    • Michejda, J.1    Kmita, H.2    Stobienia, O.3    Budzińska, M.4    Lauquin, G.J.-M.5
  • 28
    • 0030856487 scopus 로고    scopus 로고
    • The murine voltage-dependent anion channel gene family. Conserved structure and function
    • Sampson MJ, Lovell RS, Craigen WJ. (1997) The murine voltage-dependent anion channel gene family. Conserved structure and function. J Biol Chem.; 272: 18966-73.
    • (1997) J Biol Chem , vol.272 , pp. 18966-18973
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 29
    • 0017054558 scopus 로고
    • Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel
    • Schein SJ, Colombini M, Finkelstein A. (1976) Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel. 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
  • 30
    • 0034697365 scopus 로고    scopus 로고
    • Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu S, Ide T, Yanagida T, 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: 12321-5.
    • (2000) J Biol Chem , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 31
    • 0036964485 scopus 로고    scopus 로고
    • The key role of the energized state of Saccharomyces cerevisiae mitochondria in modulations of the outer membrane channels by the intermembrane space proteins
    • Stobienia O, Wróblewska S, Antos N, Budzińska M, 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: 507-16.
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 507-516
    • Stobienia, O.1    Wróblewska, S.2    Antos, N.3    Budzińska, M.4    Kmita, H.5
  • 32
    • 0036479011 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: An essential player in apoptosis
    • Tsujimoto Y, Shimizu S. (2002) The voltage-dependent anion channel: an essential player in apoptosis. Biochimie.; 84: 187-93.
    • (2002) Biochimie , vol.84 , pp. 187-193
    • Tsujimoto, Y.1    Shimizu, S.2
  • 34
    • 0032587982 scopus 로고    scopus 로고
    • Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange
    • Vander Heiden MG, Chandel NS, Schumacker PT, Thompson CB (1999) Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. Mol Cell.; 3: 159-67.
    • (1999) Mol Cell , vol.3 , pp. 159-167
    • Vander Heiden, M.G.1    Chandel, N.S.2    Schumacker, P.T.3    Thompson, C.B.4
  • 35
    • 0032765963 scopus 로고    scopus 로고
    • Mouse VDAC isoforms expressed in yeast: Channel properties and their roles in mitochondrial outer membrane permeability
    • Xu X, Decker W, Sampson MJ, Craigen WJ, 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.
    • (1999) J Membr Biol , vol.170 , pp. 89-102
    • Xu, X.1    Decker, W.2    Sampson, M.J.3    Craigen, W.J.4    Colombini, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.