메뉴 건너뛰기




Volumn 86, Issue 1 I, 2004, Pages 152-162

The Physiological Properties of A Novel Family of VDAC-Like Proteins from Drosophila melanogaster

Author keywords

[No Author keywords available]

Indexed keywords

ANION; ANION CHANNEL; CD17140 PROTEIN; CG17137 PROTEIN; CG17139 PROTEIN; DVDAC PROTEIN; LIPOSOME; PORIN; PROTEIN; UNCLASSIFIED DRUG; VDAC LIKE PROTEIN; VOLTAGE DEPENDENT ANION CHANNEL; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0346057946     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74093-X     Document Type: Article
Times cited : (33)

References (47)
  • 1
    • 0034731386 scopus 로고    scopus 로고
    • Structure and orientation of two voltage-dependent anion-selective channel isoforms. An attenuated total reflection fourier-transform infrared spectroscopy studyZ
    • Abrecht, H., E. Goormaghtigh, J. M. Ruysschaert, and F. Homble. 2000. Structure and orientation of two voltage-dependent anion-selective channel isoforms. An attenuated total reflection fourier-transform infrared spectroscopy study. J. Biol. Chem. 275:40992-40999.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40992-40999
    • Abrecht, H.1    Goormaghtigh, E.2    Ruysschaert, J.M.3    Homble, F.4
  • 2
    • 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. McCabe. 1991. Porin interaction with hexokinase and glycerol kinase: metabolic microcompartmentation at the outer mitochondrial membrane. Biochem. Med. Metab. Biol. 45:271-291.
    • (1991) Biochem. Med. Metab. Biol. , vol.45 , pp. 271-291
    • Adams, V.1    Griffin, L.2    Towbin, J.3    Gelb, B.4    Worley, K.5    McCabe, E.R.6
  • 3
    • 0035910495 scopus 로고    scopus 로고
    • Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice
    • Anflous, K., D. D. Armstrong, and W. J. Craigen. 2001. Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice. J. Biol. Chem. 276:1954-1960.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1954-1960
    • Anflous, K.1    Armstrong, D.D.2    Craigen, W.J.3
  • 4
    • 0027400112 scopus 로고
    • Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states
    • Bezrukov, S. M., and I. Vodyanoy. 1993. Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states. Biophys. J. 64:16-25.
    • (1993) Biophys. J. , vol.64 , pp. 16-25
    • Bezrukov, S.M.1    Vodyanoy, I.2
  • 5
    • 0028208520 scopus 로고
    • Human genes encoding the voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane: Mapping and identification of two new isoforms
    • Blachly-Dyson, E., A. Baldini, M. Litt, E. R. McCabe, and M. Forte. 1994. Human genes encoding the voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane: mapping and identification of two new isoforms. Genomics. 20:62-67.
    • (1994) Genomics , vol.20 , pp. 62-67
    • Blachly-Dyson, E.1    Baldini, A.2    Litt, M.3    McCabe, E.R.4    Forte, M.5
  • 7
    • 0024441078 scopus 로고
    • Probing the structure of the mitochondrial channel, VDAC, by site-directed mutagenesis: A progress report
    • Blachly-Dyson, E., S. Z. Peng, M. Colombini, and M. Forte. 1989. Probing the structure of the mitochondrial channel, VDAC, by site-directed mutagenesis: a progress report. J. Bioenerg. Biomembr. 21:471-483.
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 471-483
    • Blachly-Dyson, E.1    Peng, S.Z.2    Colombini, M.3    Forte, M.4
  • 8
    • 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
  • 9
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson, E., J. Song, W. J. Wolfgang, M. Colombini, and M. Forte. 1997. Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein. Mol. Cell. Biol. 17:5727-5738.
    • (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
  • 10
    • 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., E. B. Zambronicz, W. H. Yu, V. Adams, E. R. McCabe, J. Adelman, M. Colombini, and M. Forte. 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    Zambronicz, E.B.2    Yu, W.H.3    Adams, V.4    McCabe, E.R.5    Adelman, J.6    Colombini, M.7    Forte, M.8
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • T. Narahashi, editor. Plenum Press, New York
    • Colombini, M., E. Blachly-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    Blachly-Dyson, E.2    Forte, M.3
  • 15
    • 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., P. C. Bohni, and G. Schatz. 1982. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257:13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 16
    • 0024829374 scopus 로고
    • Characterization of the mitochondrial porin from Drosophila melanogaster
    • De Pinto, V., R. Benz, C. Caggese, and F. Palmieri. 1989. Characterization of the mitochondrial porin from Drosophila melanogaster. Biochim. Biophys. Acta. 987:1-7.
    • (1989) Biochim. Biophys. Acta , vol.987 , pp. 1-7
    • De Pinto, V.1    Benz, R.2    Caggese, C.3    Palmieri, F.4
  • 17
    • 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. Breiman. 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    Breiman, A.5
  • 18
    • 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
  • 19
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St Jean, R. A. Woods, and R. H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 20
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene. 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 21
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: Another view
    • Halestrap, A. P., G. P. McStay, and S. J. Clarke. 2002. The permeability transition pore complex: another view. Biochimie. 84:153-166.
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 22
    • 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
  • 24
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 26
    • 15644371838 scopus 로고    scopus 로고
    • The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane
    • Lee, A. C., X. Xu, E. Blachly-Dyson, M. Forte, and M. Colombini. 1998. The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane. J. Membr. Biol. 161:173-181.
    • (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
  • 27
    • 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
  • 28
    • 0029914602 scopus 로고    scopus 로고
    • Mitochondrial channels revisited
    • Mannella, C. A. 1996. Mitochondrial channels revisited. J. Bioenerg. Biomembr. 28:89-91.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 89-91
    • Mannella, C.A.1
  • 29
    • 0026591024 scopus 로고
    • Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide carrier
    • McEnery, M. W., A. M. Snowman, R. R. Trifiletti, and S. H. Snyder. 1992. Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier. Proc. Natl. Acad. Sci. USA. 89:3170-3174.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3170-3174
    • McEnery, M.W.1    Snowman, A.M.2    Trifiletti, R.R.3    Snyder, S.H.4
  • 30
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal, M., and P. Mueller. 1972. Formation of bimolecular 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
    • 0036042585 scopus 로고    scopus 로고
    • A genetic analysis of the porin gene encoding a voltage-dependent anion channel protein in Drosophila melanogaster
    • Oliva, M., V. De Pinto, P. Barsanti, and C. Caggese. 2002. A genetic analysis of the porin gene encoding a voltage-dependent anion channel protein in Drosophila melanogaster. Mol. Genet. Genomics. 267:746-756.
    • (2002) Mol. Genet. Genomics , vol.267 , pp. 746-756
    • Oliva, M.1    De Pinto, V.2    Barsanti, P.3    Caggese, C.4
  • 33
    • 0029854155 scopus 로고    scopus 로고
    • ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane
    • Rostovtseva, T. K., 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.K.1    Colombini, M.2
  • 34
    • 0036219774 scopus 로고    scopus 로고
    • Dynamics of nucleotides in VDAC channels: Structure-specific noise generation
    • Rostovtseva, T. K., A. Komarov, S. M. Bezrukov, and M. Colombini. 2002. Dynamics of nucleotides in VDAC channels: structure-specific noise generation. Biophys. J. 82:193-205.
    • (2002) Biophys. J. , vol.82 , pp. 193-205
    • Rostovtseva, T.K.1    Komarov, A.2    Bezrukov, S.M.3    Colombini, M.4
  • 36
    • 0030792532 scopus 로고    scopus 로고
    • Cloning and molecular characterization of a voltage-dependent anion-selective channel (VDAC) from Drosophila melanogaster
    • Ryerse, J., E. Blachly-Dyson, M. Forte, and B. Nagel. 1997. Cloning and molecular characterization of a voltage-dependent anion-selective channel (VDAC) from Drosophila melanogaster. Biochim. Biophys. Acta. 1327:204-212.
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 204-212
    • Ryerse, J.1    Blachly-Dyson, E.2    Forte, M.3    Nagel, B.4
  • 38
    • 0030856487 scopus 로고    scopus 로고
    • The murine voltage-dependent anion channel gene family. Conserved structure and function
    • Sampson, M. J., R. S. Lovell, and W. J. Craigen. 1997. The murine voltage-dependent anion channel gene family. Conserved structure and function. J. Biol. Chem. 272:18966-18973.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18966-18973
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 39
    • 0030586893 scopus 로고    scopus 로고
    • A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8
    • Sampson, M. J., R. S. Lovell, D. B. Davison, and W. J. Craigen. 1996. A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8. Genomics. 36:192-196.
    • (1996) Genomics , vol.36 , pp. 192-196
    • Sampson, M.J.1    Lovell, R.S.2    Davison, D.B.3    Craigen, W.J.4
  • 41
    • 0031806216 scopus 로고    scopus 로고
    • The sensor regions of VDAC are translocated from within the membrane to the surface during the gating processes
    • Song, J., C. Midson, E. Blachly-Dyson, M. Forte, and M. Colombini. 1998b. The sensor regions of VDAC are translocated from within the membrane to the surface during the gating processes. Biophys. J. 74:2926-2944.
    • (1998) Biophys. J. , vol.74 , pp. 2926-2944
    • Song, J.1    Midson, C.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 42
    • 0037249406 scopus 로고    scopus 로고
    • The FlyBase database of the Drosophila genome projects and community literature
    • The-FlyBase-Consortium. 2003. The FlyBase database of the Drosophila genome projects and community literature. Nucleic Acids Res. 31:172-175.
    • (2003) Nucleic Acids Res , vol.31 , pp. 172-175
  • 43
    • 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
  • 47
    • 0032765963 scopus 로고    scopus 로고
    • Mouse VDAC isoforms expressed in yeast: Channel properties and their roles in mitochondrial outer membrane permeability
    • Xu, X., W. Decker, M. J. Sampson, W. J. Craigen, and M. Colombini. 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.