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Volumn 17, Issue 10, 1997, Pages 5727-5738

Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein

Author keywords

[No Author keywords available]

Indexed keywords

ANION CHANNEL; MEMBRANE PROTEIN;

EID: 0030873947     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.10.5727     Document Type: Article
Times cited : (143)

References (32)
  • 1
    • 0025796715 scopus 로고
    • Porin interaction with hexokinase and glycerol kinase: Metabolic microcompartmentation at the outer mitochondrial membrane
    • Adams, V., L. Griffin, J. Towbin, B. Gelb, K. Worley, and E. R. B. McCabe. 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
    • 0025055329 scopus 로고
    • The cationically selective state of the mitochondrial outer membrane porc: A study with intact mitochondria and reconstituted mitochondrial porin
    • Benz, R., M. Kottke, and D. Brdiczka. 1990. The cationically selective state of the mitochondrial outer membrane porc: 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    Kottke, M.2    Brdiczka, D.3
  • 4
    • 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
  • 5
    • 0027389308 scopus 로고
    • Cloning and functonal expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel
    • Blachly-Dyson, E., E. B. Zambronicz, W. Yu, V. Adams, E. R. B. McCabe, J. Adelman, M. Colombini, and M. Forte. 1993. Cloning and functonal 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    Zambronicz, E.B.2    Yu, W.3    Adams, V.4    McCabe, E.R.B.5    Adelman, J.6    Colombini, M.7    Forte, M.8
  • 6
    • 0020640158 scopus 로고
    • Construction of high copy yeast vectors using 2-μM circle sequences
    • Broach, J. R. 1983. Construction of high copy yeast vectors using 2-μM circle sequences. Methods Enzymol. 101:307-325.
    • (1983) Methods Enzymol. , vol.101 , pp. 307-325
    • Broach, J.R.1
  • 7
    • 0018956403 scopus 로고
    • Pore size and properties of channels from mitochondria isolated from Neurospora crassa
    • Colombini, M. 1980. Pore size and properties of channels from mitochondria isolated from Neurospora crassa. J. Membr. Biol. 53:79-84.
    • (1980) J. Membr. Biol. , vol.53 , pp. 79-84
    • Colombini, M.1
  • 8
    • 0005704279 scopus 로고
    • Modulation of the mitochondrial channel VDAC by a variety of agents
    • A. Azzi (ed.), Springer-Verlag KG, Berlin, Germany
    • Colombini, M., M. J. Holden, and P. S. Mangan. 1989. Modulation of the mitochondrial channel VDAC by a variety of agents, p. 215-224. In A. Azzi (ed.), Anion carriers of mitochondrial membranes. Springer-Verlag KG, Berlin, Germany.
    • (1989) Anion Carriers of Mitochondrial Membranes , pp. 215-224
    • Colombini, M.1    Holden, M.J.2    Mangan, P.S.3
  • 9
    • 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., K. Suda, and G. Schatz. 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
  • 10
    • 0029379612 scopus 로고
    • Multiple cDNAs of wheat voltage-dependent anion channels (VDAC): Isolation, differential expression, mapping and evolution
    • Elkeles, A., K. M. Devos, D. Graur, M. Zizi, and A. Breimann. 1995. Multiple cDNAs of wheat voltage-dependent anion channels (VDAC): Isolation, differential expression, mapping and evolution. Plant Mol. Biol. 29:109-124.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 109-124
    • Elkeles, A.1    Devos, K.M.2    Graur, D.3    Zizi, M.4    Breimann, A.5
  • 11
    • 0022590783 scopus 로고
    • The amino terminus of the yeast F1-ATPase beta-subunit functions as a mitochondrial import signal
    • Emr, S. D., A. Vassarotti, J. Garrett, B. L. Geller, M. Takeda, and M. G. Douglas. 1986. The amino terminus of the yeast F1-ATPase beta-subunit functions as a mitochondrial import signal. J. Cell Biol. 102:523-533.
    • (1986) J. Cell Biol. , vol.102 , pp. 523-533
    • Emr, S.D.1    Vassarotti, A.2    Garrett, J.3    Geller, B.L.4    Takeda, M.5    Douglas, M.G.6
  • 12
    • 85036488362 scopus 로고    scopus 로고
    • Unpublished observation
    • 10a. Forte, M. Unpublished observation.
    • Forte, M.1
  • 13
    • 0023392255 scopus 로고
    • Molecular genetics of the VDAC ion channel: Structural model and sequence analysis
    • Forte, M., H. R. Guy, and C. A. Mannella. 1987. Molecular genetics of the VDAC ion channel: structural model and sequence analysis. J. Bioenerg. Biomembr. 19:341-350.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 341-350
    • Forte, M.1    Guy, H.R.2    Mannella, C.A.3
  • 14
    • 0029984773 scopus 로고    scopus 로고
    • Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
    • Goodson, H. V., B. L. Anderson, H. M. Warrick, L. A. Pon, and J. A. Spudich. 1996. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J. Cell Biol. 133:1277-1291.
    • (1996) J. Cell Biol. , vol.133 , pp. 1277-1291
    • Goodson, H.V.1    Anderson, B.L.2    Warrick, H.M.3    Pon, L.A.4    Spudich, J.A.5
  • 15
    • 0028800976 scopus 로고
    • Isolation of highly purified mitochondria from Saccharomyces cerevisiae
    • Glick, B. S., and L. A. Pon. 1995. Isolation of highly purified mitochondria from Saccharomyces cerevisiae. Methods Enzymol. 213-223.
    • (1995) Methods Enzymol. , pp. 213-223
    • Glick, B.S.1    Pon, L.A.2
  • 16
    • 0027159339 scopus 로고
    • Mitochondrial porin cDNA predicts the existence of multiple human porins
    • Ha, H., P. Hajek, D. M. Bedwell, and P. D. Burrows. 1993. Mitochondrial porin cDNA predicts the existence of multiple human porins. J. Biol. Chem. 268:12143-12149.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12143-12149
    • Ha, H.1    Hajek, P.2    Bedwell, D.M.3    Burrows, P.D.4
  • 17
    • 0028079979 scopus 로고
    • Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria
    • Heins, L., H. Mentzel, A. Schmid, R. Benz, and U. K. Schmitz. 1994. Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria. J. Biol. Chem. 269:26402-26410.
    • (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
  • 18
    • 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
  • 20
    • 0030050144 scopus 로고    scopus 로고
    • Identification of porin as a binding site for MAP2
    • Linden, M., and G. Karlsson. 1996. Identification of porin as a binding site for MAP2. Biochem. Biophys. Res. Commun. 218:833-836.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 833-836
    • Linden, M.1    Karlsson, G.2
  • 21
    • 0001246788 scopus 로고    scopus 로고
    • Ion channels of mitochondrial membranes
    • Mannella, C., and C. Kinally. 1997. Ion channels of mitochondrial membranes. Biomembranes 6:377-410.
    • (1997) Biomembranes , vol.6 , pp. 377-410
    • Mannella, C.1    Kinally, C.2
  • 22
    • 0020450839 scopus 로고
    • Structure of the outer mitochondrial membrane: Ordered arrays of porelike subunits in outer-membrane fractions from Neurospora crassa mitochondria
    • Mannella, C. A. 1982. Structure of the outer mitochondrial membrane: ordered arrays of porelike 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.A.1
  • 23
    • 0022033632 scopus 로고
    • Molecular cloning and sequencing of cDNA for yeast porin, an outer mitochondrial membrane protein: A search for targeting signal in the primary structure
    • Mihara, K., and R. Sato. 1985. Molecular cloning and sequencing of cDNA for yeast porin, an outer mitochondrial membrane protein: a search for targeting signal in the primary structure. EMBO J. 4:769-774.
    • (1985) EMBO J. , vol.4 , pp. 769-774
    • Mihara, K.1    Sato, R.2
  • 24
    • 0029018094 scopus 로고
    • Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy
    • Reymann, S., H. Florke, M. Heiden, C. Jakob, U. Stadtmuller, P. Steinacker, V. E. Lalk, I. Pardowitz, and F. P. Thinnes. 1995. Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy. Biochem. Mol. Med. 54:75-87.
    • (1995) Biochem. Mol. Med. , vol.54 , pp. 75-87
    • Reymann, S.1    Florke, H.2    Heiden, M.3    Jakob, C.4    Stadtmuller, U.5    Steinacker, P.6    Lalk, V.E.7    Pardowitz, I.8    Thinnes, F.P.9
  • 25
    • 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
  • 26
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 202-209.
    • (1983) Methods Enzymol. , pp. 202-209
    • Rothstein, R.J.1
  • 27
    • 85036491745 scopus 로고    scopus 로고
    • Cloning and molecular characterization of a voltage dependent anion-selective channel (VDAC) from Drosophila melanogaster
    • in press
    • Ryerse, J., E. Blachly-Dyson, M. Forte, and B. Nagel. Cloning and molecular characterization of a voltage dependent anion-selective channel (VDAC) from Drosophila melanogaster. Biochim. Biophys. Acta, in press.
    • Biochim. Biophys. Acta
    • Ryerse, J.1    Blachly-Dyson, E.2    Forte, M.3    Nagel, B.4
  • 28
    • 0029925099 scopus 로고    scopus 로고
    • Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms
    • Sampson, M. J., R. S. Lovell, and W. J. Craigen. 1996. Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms. Genomics 33:283-288.
    • (1996) Genomics , vol.33 , pp. 283-288
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 29
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R. H., and R. D. Gietz. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16:339-346.
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 30
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L. F., and M. P. Yaffe. 1994. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 126:1361-1373.
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 31
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • Yaffe, M. P., and G. Schatz. 1984. Two nuclear mutations that block mitochondrial protein import in yeast. Proc. Natl. Acad. Sci. USA 81:4819-4823.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2
  • 32
    • 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


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