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Volumn 145, Issue 5, 1999, Pages 973-978

Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20

Author keywords

Import; Mitochondria; Porin; Tom20; Voltage dependent anion selective channel

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANION CHANNEL; LIPOSOME; MUTANT PROTEIN; PORIN; PROTEIN PRECURSOR; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0033620612     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.145.5.973     Document Type: Article
Times cited : (53)

References (38)
  • 1
    • 0023513271 scopus 로고
    • The mitochondrial outer membrane channel. VDAC, is regulaled by a synthetic polyamon
    • Colombini, M., C.L. Yeung, J. Tung, and T. Konig. 1987. The mitochondrial outer membrane channel. VDAC, is regulaled by a synthetic polyamon. 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    Konig, T.4
  • 2
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • Colombini, M., D.E. Blachly, and M. Forte. 1996. VDAC, a channel in the outer mitochondrial membrane. Ion Channels. 4:169-202.
    • (1996) Ion Channels , vol.4 , pp. 169-202
    • Colombini, M.1    Blachly, D.E.2    Forte, M.3
  • 3
    • 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    Bohni, P.C.2    Schatz, G.3
  • 4
    • 0031551023 scopus 로고    scopus 로고
    • Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane
    • de Kroon, A., D. Dolis, A. Mayer, R. Lill, and K.B. de Kruijff. 1997. Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane. Biochim. Biophys. Acta. 1325:108-116.
    • (1997) Biochim. Biophys. Acta , vol.1325 , pp. 108-116
    • De Kroon, A.1    Dolis, D.2    Mayer, A.3    Lill, R.4    De Kruijff, K.B.5
  • 5
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers, M., and G. Schatz. 1986. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature. 322:228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 6
    • 0020039867 scopus 로고
    • Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: Comparison with endoplasmic reticulum and mitochondrial membrane
    • Fujiki, Y., S. Fowler, H. Shio, A.L. Hubbard, and P. Lazarow. 1982. Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membrane. J. Cell Biol. 93:103-110.
    • (1982) J. Cell Biol. , vol.93 , pp. 103-110
    • Fujiki, Y.1    Fowler, S.2    Shio, H.3    Hubbard, A.L.4    Lazarow, P.5
  • 7
    • 0029091583 scopus 로고
    • Identification of the human mitochondrial protein import receptor, huMas20p
    • Goping, I.S., D.G. Millar, and G.C. Shore. 1995. Identification of the human mitochondrial protein import receptor, huMas20p. FEBS Lett. 373:45-50.
    • (1995) FEBS Lett. , vol.373 , pp. 45-50
    • Goping, I.S.1    Millar, D.G.2    Shore, G.C.3
  • 9
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D.R., and J.C. Reed. 1998. Mitochondria and apoptosis. Science. 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 10
    • 0031106617 scopus 로고    scopus 로고
    • Import of proteins into mitochondria and chloroplasts
    • Haucke, V., and G. Schatz. 1997. Import of proteins into mitochondria and chloroplasts. Trends Cell Biol. 7:103-106.
    • (1997) Trends Cell Biol. , vol.7 , pp. 103-106
    • Haucke, V.1    Schatz, G.2
  • 11
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill, K., K. Model, M.T. Ryan, K. Dietmeimer, F. Martin, R. Wagner, and N. Pfanner. 1998. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature. 395:516-521.
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeimer, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 12
    • 0029129982 scopus 로고
    • RPM2, independently of its mitochondrial RNAse P function. Suppresses an ISP42 mutant defective in mitochondrial import and is essential for normal growth
    • Kassenbrock, C.K., G.J. Gao, K.R. Groom, P. Sulo, M.G. Douglas, and N.C. Martin. 1995. RPM2, independently of its mitochondrial RNAse P function. suppresses an ISP42 mutant defective in mitochondrial import and is essential for normal growth. Mol. Cell. Biol. 15:4763-4770.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4763-4770
    • Kassenbrock, C.K.1    Gao, G.J.2    Groom, K.R.3    Sulo, P.4    Douglas, M.G.5    Martin, N.C.6
  • 14
    • 15644371838 scopus 로고    scopus 로고
    • The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane
    • Lee, A.C., X. Xu, D.E. Blachly, 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, D.E.3    Forte, M.4    Colombini, M.5
  • 15
    • 0026755435 scopus 로고
    • Reversal of the orientation of an integral protein of the mitochondrial outer membrane
    • Li, J.M., and G.C. Shore. 1992. Reversal of the orientation of an integral protein of the mitochondrial outer membrane. Science. 256:1815-1817.
    • (1992) Science , vol.256 , pp. 1815-1817
    • Li, J.M.1    Shore, G.C.2
  • 16
    • 0031448082 scopus 로고    scopus 로고
    • On the structure and gating mechanism of the mitochondrial channel, VDAC
    • Mannella, C.A. 1997. On the structure and gating mechanism of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 29:525-531.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 525-531
    • Mannella, C.A.1
  • 17
    • 0027049521 scopus 로고
    • A signal-anchor sequence selective for the mitochondrial outer membrane
    • McBride, H.M., D.G. Millar, J.M. Li, and G.C. Shore. 1992. A signal-anchor sequence selective for the mitochondrial outer membrane. J. Cell Biol. 119: 1451-1457.
    • (1992) J. Cell Biol. , vol.119 , pp. 1451-1457
    • McBride, H.M.1    Millar, D.G.2    Li, J.M.3    Shore, G.C.4
  • 18
    • 8944248278 scopus 로고    scopus 로고
    • The human mitochondrial import receptor, hTom20p, prevents a cryptic matrix targeting sequence from gaining access to the protein translocation machinery
    • McBride, H.M., I.S. Goping, and G.C. Shore. 1996. The human mitochondrial import receptor, hTom20p, prevents a cryptic matrix targeting sequence from gaining access to the protein translocation machinery. J. Cell Biol. 134: 370-313.
    • (1996) J. Cell Biol. , vol.134 , pp. 370-1313
    • McBride, H.M.1    Goping, I.S.2    Shore, G.C.3
  • 19
    • 0029909757 scopus 로고    scopus 로고
    • Signal anchor sequence insertion into the outer mitochondrial membrane. Comparison with porin and the matrix targeting pathway
    • Millar, D.G., and G.C. Shore. 1996. Signal anchor sequence insertion into the outer mitochondrial membrane. Comparison with porin and the matrix targeting pathway. J. Biol. Chem. 271:25823-25829.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25823-25829
    • Millar, D.G.1    Shore, G.C.2
  • 20
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66: 863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 21
    • 0023891819 scopus 로고
    • Protein sorting between mitochondrial membranes specified by position of the stop-transfer domain
    • Nguyen, M., A.W. Bell, and G.C. Shore. 1988. Protein sorting between mitochondrial membranes specified by position of the stop-transfer domain. J. Cell Biol. 106:1499-1505.
    • (1988) J. Cell Biol. , vol.106 , pp. 1499-1505
    • Nguyen, M.1    Bell, A.W.2    Shore, G.C.3
  • 22
    • 0030910776 scopus 로고    scopus 로고
    • The Tom and Tim machine
    • Pfanner, N., and M. Meijer. 1997. The Tom and Tim machine. Curr. Biol. 7:R100-R103.
    • (1997) Curr. Biol. , vol.7
    • Pfanner, N.1    Meijer, M.2
  • 25
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T., A.B. Jungnickel, and U. Kutay. 1996. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65:271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.1    Jungnickel, A.B.2    Kutay, U.3
  • 26
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function
    • Rostovtseva, T., and M. Colombini. 1997. VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys. J. 72:1954-1962.
    • (1997) Biophys. J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 27
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and B. Dobberstein. 1996. Common principles of protein translocation across membranes. Science. 271:1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 28
    • 0032558380 scopus 로고    scopus 로고
    • Functional and structural properties of the mitochondrial outer membrane receptor Tom20
    • Schleiff, E., and J.L. Turnbull. 1998. Functional and structural properties of the mitochondrial outer membrane receptor Tom20. Biochemistry. 37:13043-13051.
    • (1998) Biochemistry , vol.37 , pp. 13043-13051
    • Schleiff, E.1    Turnbull, J.L.2
  • 29
    • 0030791131 scopus 로고    scopus 로고
    • Interactions of the human mitochondrial protein import receptor, hTom20. With precursor proteins in vitro reveal pleiotropic specificities and different receptor domain requirements
    • Schleiff, E., G.C. Shore, and I.S. Coping. 1997. Interactions of the human mitochondrial protein import receptor, hTom20. with precursor proteins in vitro reveal pleiotropic specificities and different receptor domain requirements. J. Biol. Chem. 272:17784-17789.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17784-17789
    • Schleiff, E.1    Shore, G.C.2    Coping, I.S.3
  • 30
    • 0028882571 scopus 로고
    • A novel strategy affords high-yield coupling of antibody Fab' fragments to liposomes
    • Shahinian, S., and J.R. Silvius. 1995 A novel strategy affords high-yield coupling of antibody Fab' fragments to liposomes. Biochim. Biophys. Acta. 1239:157-167.
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 157-167
    • Shahinian, S.1    Silvius, J.R.2
  • 31
    • 0025295174 scopus 로고
    • Mitochondrial precursor protein. Effects of 70-kilodalton heat shock protein on polypeptide folding, aggregation, and import competence
    • Sheffield, W.P., G.C. Shore, and S.K. Randall. 1990. Mitochondrial precursor protein. Effects of 70-kilodalton heat shock protein on polypeptide folding, aggregation, and import competence. J. Biol. Chem. 265:11069-11076.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11069-11076
    • Sheffield, W.P.1    Shore, G.C.2    Randall, S.K.3
  • 32
    • 0028149597 scopus 로고
    • Rupture of the mitochondrial outer membrane impairs porin assembly
    • Smith, M., S. Hicks, K. Baker, and R. McCauley. 1994. Rupture of the mitochondrial outer membrane impairs porin assembly. J. Biol. Chem. 269: 28460-28464.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28460-28464
    • Smith, M.1    Hicks, S.2    Baker, K.3    McCauley, R.4
  • 33
    • 0024801086 scopus 로고
    • MOM19, an import receptor for mitochondrial precursor proteins
    • Sollner, T., G. Griffiths, R. Pfaller, N. Pfanner, and W. Neupert. 1989. MOM19, an import receptor for mitochondrial precursor proteins. Cell, 59:1061-1070.
    • (1989) Cell , vol.59 , pp. 1061-1070
    • Sollner, T.1    Griffiths, G.2    Pfaller, R.3    Pfanner, N.4    Neupert, W.5
  • 34
    • 0029034341 scopus 로고
    • Peptide-specific antibodies as probes of the topography of the voltage gated channel of the mitochondrial outer membrane of Neurospora crassa
    • Stanley, S.J., A. Dias, D. D'Arcangelis, and C.A. Mannella. 1995. Peptide-specific antibodies as probes of the topography of the voltage gated channel of the mitochondrial outer membrane of Neurospora crassa. J. Biol. Chem. 270: 16694-16700.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16694-16700
    • Stanley, S.J.1    Dias, A.2    D'Arcangelis, D.3    Mannella, C.A.4
  • 35
    • 0024424988 scopus 로고
    • A 42K outer membrane protein is a component of the yeast mitochondrial protein import site
    • Vestweber, D., J. Brunner, A. Baker, and G. Schatz. 1989. A 42K outer membrane protein is a component of the yeast mitochondrial protein import site. Nature. 341:205-209.
    • (1989) Nature , vol.341 , pp. 205-209
    • Vestweber, D.1    Brunner, J.2    Baker, A.3    Schatz, G.4
  • 36
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss, M.S., U. Abele, J. Weckesser, W. Welte, E. Schiltz, and G.E. Schultz. 1991. Molecular architecture and electrostatic properties of a bacterial porin. Science. 254:1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schultz, G.E.6
  • 37
    • 0029841640 scopus 로고    scopus 로고
    • Self-catalyzed insertion of proteins into phospholipid membranes
    • Xu, X., and M. Colombini. 1996. Self-catalyzed insertion of proteins into phospholipid membranes. J. Biol. Chem. 271:23675-23682.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23675-23682
    • Xu, X.1    Colombini, M.2
  • 38
    • 0028158479 scopus 로고
    • NADH regulates the gating of VDAC, the mitochondrial outer membrane channel
    • Zizi, M., M. Forte, D.E. Blachly, 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, D.E.3    Colombini, M.4


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