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Volumn 8, Issue 12, 2013, Pages

The Voltage-Dependent Anion selective Channel 1 (VDAC1) topography in the mitochondrial outer membrane as detected in intact cell

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; HEXOKINASE; PROTEIN BCL 2; VOLTAGE DEPENDENT ANION CHANNEL 1;

EID: 84891905707     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0081522     Document Type: Article
Times cited : (61)

References (38)
  • 1
    • 77952886494 scopus 로고    scopus 로고
    • VDAC, a multi-functional mitochondrial protein regulating cell life and death
    • doi:10.1016/j.mam.2010.03.002. PubMed: 20346371
    • Shoshan-Barmatz V, De Pinto V, Zweckstetter M, Raviv Z, Keinan N et al. (2010) VDAC, a multi-functional mitochondrial protein regulating cell life and death. Mol Aspects Med 31: 227-285. doi:10.1016/j.mam.2010.03.002. PubMed: 20346371.
    • (2010) Mol Aspects Med , vol.31 , pp. 227-285
    • Shoshan-Barmatz, V.1    De Pinto, V.2    Zweckstetter, M.3    Raviv, Z.4    Keinan, N.5
  • 3
    • 0030947935 scopus 로고    scopus 로고
    • Vdac channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function
    • Rostovtseva T, Colombini M (1997) VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys J 72: 1954-1962. doi:10.1016/S0006-3495(97)78841-6. PubMed: 9129800. (Pubitemid 27184425)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 4
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • DOI 10.1152/physrev.00013.2006
    • Kroemer G, Galluzzi L, Brenner C (2007) Mitochondrial Membrane Permeabilization in Cell Death. Physiol Rev 87: 99-163. doi:10.1152/physrev. 00013.2006. PubMed: 17237344. (Pubitemid 46209992)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 5
  • 6
    • 84875233751 scopus 로고    scopus 로고
    • VDAC1: From structure to cancer therapy Front
    • Shoshan-Barmatz V, Mizrachi D (2012) VDAC1: from structure to cancer therapy Front. Oncol 2: 164.
    • (2012) Oncol , vol.2 , pp. 164
    • Shoshan-Barmatz, V.1    Mizrachi, D.2
  • 7
    • 0027930089 scopus 로고
    • Lack of voltage-dependent anion channel in human mitochondrial myopathies [26]
    • Huizing M, Ruitenbeek W, Thinnes F, De Pinto V (1994) Deficiency of the Voltage-Dependent Anion Channel (VDAC): a novel cause of mitochondrial myopathies. Lancet 344: 762. doi:10.1016/S0140-6736(94)92258-6. (Pubitemid 24281455)
    • (1994) Lancet , vol.344 , Issue.8924 , pp. 762
    • Huizing, M.1    Ruitenbeek, W.2    Thinnes, F.P.3    DePinto, V.4
  • 8
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • doi:10.1126/science.1161302. PubMed: 18755977
    • Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G (2008) Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 321: 1206-1210. doi:10.1126/science.1161302. PubMed: 18755977.
    • (2008) Science , vol.321 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6
  • 9
    • 55749094704 scopus 로고    scopus 로고
    • Structure of the human voltage-dependent anion channel
    • doi:10.1073/pnas.0808115105. PubMed: 18832158
    • Bayrhuber M, Meins T, Habeck M, Becker S, Giller K et al. (2008) Structure of the human voltage-dependent anion channel. Proc Natl Acad Sci U S A 105: 15370-15375. doi:10.1073/pnas.0808115105. PubMed: 18832158.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15370-15375
    • Bayrhuber, M.1    Meins, T.2    Habeck, M.3    Becker, S.4    Giller, K.5
  • 10
    • 56649099192 scopus 로고    scopus 로고
    • The crystal structure of mouse VDAC1 at 2.3 angstrom resolution reveals mechanistic insights into metabolite gating
    • doi:10.1073/pnas.0809634105. PubMed: 18988731
    • Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J et al. (2008) The crystal structure of mouse VDAC1 at 2.3 angstrom resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci U S A 105: 17742-17747. doi:10.1073/pnas.0809634105. PubMed: 18988731.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17742-17747
    • Ujwal, R.1    Cascio, D.2    Colletier, J.P.3    Faham, S.4    Zhang, J.5
  • 11
    • 68249126139 scopus 로고    scopus 로고
    • The published 3D structure of the VDAC channel: Native or not?
    • doi:10.1016/j.tibs.2009.05.001. PubMed: 19647437
    • Colombini M (2009) The published 3D structure of the VDAC channel: native or not? Trends Biochem Sci 34: 382-389. doi:10.1016/j.tibs.2009.05.001. PubMed: 19647437.
    • (2009) Trends Biochem Sci , vol.34 , pp. 382-389
    • Colombini, M.1
  • 12
    • 77956190164 scopus 로고    scopus 로고
    • The 3D structures of VDAC represent a native conformation
    • doi:10.1016/j.tibs.2010.03.005. PubMed: 20708406
    • Hiller S, Abramson J, Mannella C, Wagner G, Zeth K (2010) The 3D structures of VDAC represent a native conformation. Trends Biochem Sci 35: 514-521. doi:10.1016/j.tibs.2010.03.005. PubMed: 20708406.
    • (2010) Trends Biochem Sci , vol.35 , pp. 514-521
    • Hiller, S.1    Abramson, J.2    Mannella, C.3    Wagner, G.4    Zeth, K.5
  • 13
    • 0025788323 scopus 로고
    • Peptidespecific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin
    • doi:10.1021/bi00106a017. PubMed: 1718414
    • De Pinto V, Prezioso G, Thinnes F, Link TA, Palmieri F (1991) Peptidespecific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin. Biochemistry 30: 10191-10200. doi:10.1021/bi00106a017. PubMed: 1718414.
    • (1991) Biochemistry , vol.30 , pp. 10191-10200
    • De Pinto, V.1    Prezioso, G.2    Thinnes, F.3    Link, T.A.4    Palmieri, F.5
  • 14
    • 0029034341 scopus 로고
    • Peptidespecific antibodies as probes of the topography of the voltage-gated channel in the mitochondrial outer membrane of Neurospora crassa
    • doi:10.1074/jbc.270.28.16694. PubMed: 7542652
    • Stanley S, Dias JA, D'Arcangelis D, Mannella CA (1995) Peptidespecific antibodies as probes of the topography of the voltage-gated channel in the mitochondrial outer membrane of Neurospora crassa. J Biol Chem 270: 16694-16700. doi:10.1074/jbc.270.28.16694. PubMed: 7542652.
    • (1995) J Biol Chem , vol.270 , pp. 16694-16700
    • Stanley, S.1    Dias, J.A.2    D'arcangelis, D.3    Mannella, C.A.4
  • 15
    • 59849116432 scopus 로고    scopus 로고
    • Probing the orientation of yeast VDAC1 in vivo
    • doi: 10.1016/j.febslet.2009.01.039. PubMed: 19185576
    • McDonald BM, Wydro MM, Lightowlers RN, Lakey JH (2009) Probing the orientation of yeast VDAC1 in vivo. FEBS Lett 583: 739-742. doi: 10.1016/j.febslet.2009.01.039. PubMed: 19185576.
    • (2009) FEBS Lett , vol.583 , pp. 739-742
    • McDonald, B.M.1    Wydro, M.M.2    Lightowlers, R.N.3    Lakey, J.H.4
  • 16
    • 52449119836 scopus 로고    scopus 로고
    • Regulation of hexokinase binding to VDAC
    • doi:10.1007/s10863-008-9148-8. PubMed: 18683036
    • Pastorino JG, Hoek JB (2008) Regulation of hexokinase binding to VDAC. J Bioenerg Biomembr 40: 171-178. doi:10.1007/s10863-008-9148-8. PubMed: 18683036.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 171-178
    • Pastorino, J.G.1    Hoek, J.B.2
  • 17
    • 84862156776 scopus 로고    scopus 로고
    • Structure-based analysis of VDAC1: N-terminus location, translocation, channel gating and association with anti-apoptotic proteins
    • doi:10.1042/BJ20112079. PubMed: 22397371
    • Geula S, Ben-Hail D, Shoshan-Barmatz V (2012) Structure-based analysis of VDAC1: N-terminus location, translocation, channel gating and association with anti-apoptotic proteins. Biochem J 444: 475-485. doi:10.1042/BJ20112079. PubMed: 22397371.
    • (2012) Biochem J , vol.444 , pp. 475-485
    • Geula, S.1    Ben-Hail, D.2    Shoshan-Barmatz, V.3
  • 18
    • 73249133403 scopus 로고    scopus 로고
    • Recombinant differential anchorage probes that tower over the spatial dimension of intracellular signals for high content screening and analysis
    • doi: 10.1021/ac9015227. PubMed: 19873978
    • Schembri L, Zanese M, Depierre-Plinet G, Petit M, Elkaoukabi-Chaibi A, Tauzin L et al. (2009) Recombinant differential anchorage probes that tower over the spatial dimension of intracellular signals for high content screening and analysis. Anal Chem 81: 9590-9598. doi: 10.1021/ac9015227. PubMed: 19873978.
    • (2009) Anal Chem , vol.81 , pp. 9590-9598
    • Schembri, L.1    Zanese, M.2    Depierre-Plinet, G.3    Petit, M.4    Elkaoukabi-Chaibi, A.5    Tauzin, L.6
  • 19
    • 0035159675 scopus 로고    scopus 로고
    • Targeting of a tail-anchored protein to endoplasmic reticulum and outer membrane by independent but competing pathways
    • Borgese N, Gazzoni I, Barberi M, Colombo S, Pedrazzini E (2001) Targeting of a tail-anchored protein to endoplasmic reticulum and mitochondrial outer membrane by independent but competing pathways. Mol Biol Cell 12: 2482-2496. doi:10.1091/mbc.12.8.2482. PubMed: 11514630. (Pubitemid 33051970)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2482-2496
    • Borgese, N.1    Gazzoni, I.2    Barberi, M.3    Colombo, S.4    Pedrazzini, E.5
  • 20
    • 33646357780 scopus 로고    scopus 로고
    • Fluorescence protease protection of GFP chimeras to reveal protein topology and subcellular localization
    • doi:10.1038/nmeth857. PubMed: 16489338
    • Lorenz H, Hailey DW, Lippincott-Schwartz J (2006) Fluorescence protease protection of GFP chimeras to reveal protein topology and subcellular localization. Nat Methods 3: 205-210. doi:10.1038/nmeth857. PubMed: 16489338.
    • (2006) Nat Methods , vol.3 , pp. 205-210
    • Lorenz, H.1    Hailey, D.W.2    Lippincott-Schwartz, J.3
  • 21
    • 71749121777 scopus 로고    scopus 로고
    • Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo durings stress-induced apoptosis
    • doi:10.1038/cr.2009.98. PubMed: 19668262
    • Tomasello F, Messina A, Lartigue L, Schembri L, Medina C, Reina S et al. (2009) Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo durings stress-induced apoptosis. Cell Res 19: 1363-1376. doi:10.1038/cr.2009.98. PubMed: 19668262.
    • (2009) Cell Res , vol.19 , pp. 1363-1376
    • Tomasello, F.1    Messina, A.2    Lartigue, L.3    Schembri, L.4    Medina, C.5    Reina, S.6
  • 22
    • 0037421221 scopus 로고    scopus 로고
    • Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
    • DOI 10.1083/jcb.200208089
    • Ricci JE, Gottlieb RA, Green DR (2003) Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis. J Cell Biol 160: 65-75. doi:10.1083/jcb.200208089. PubMed: 12515825. (Pubitemid 36091717)
    • (2003) Journal of Cell Biology , vol.160 , Issue.1 , pp. 65-75
    • Ricci, J.-E.1    Gottlieb, R.A.2    Green, D.R.3
  • 23
    • 33947430496 scopus 로고    scopus 로고
    • The HA tag is cleaved and loses immunoreactivity during apoptosis
    • DOI 10.1038/nmeth0207-107, PII NMETH0207-107
    • Schembri L, Dalibart R, Tomasello F, Legembre P, Ichas F et al. (2007) The HA tag is cleaved and loses immunoreactivity during apoptosis. Nat Methods. 4: 107-108. doi:10.1038/nmeth0207-107. PubMed: 17264856. (Pubitemid 46454672)
    • (2007) Nature Methods , vol.4 , Issue.2 , pp. 107-108
    • Schembri, L.1    Dalibart, R.2    Tomasello, F.3    Legembre, P.4    Ichas, F.5    De Giorgi, F.6
  • 25
    • 0026439921 scopus 로고
    • Morphological analysis of protein transport from the ER to Golgi membranes in Digitonin-permeabilized cells: Role of the P58 containing compartment
    • doi:10.1083/jcb.119.5.1097. PubMed: 1447290
    • Plutner H, Davidson HW, Saraste J, Balch WE (1992) Morphological analysis of protein transport from the ER to Golgi membranes in Digitonin-permeabilized cells: role of the P58 containing compartment. J Cell Biol 119: 1097-1116. doi:10.1083/jcb.119.5.1097. PubMed: 1447290.
    • (1992) J Cell Biol , vol.119 , pp. 1097-1116
    • Plutner, H.1    Davidson, H.W.2    Saraste, J.3    Balch, W.E.4
  • 26
    • 77953811604 scopus 로고    scopus 로고
    • Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology
    • doi:10.1016/j.bbabio.2010.04.019. PubMed: 20450883
    • Zeth K (2010) Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology. Biochim Biophys Acta 1797: 1292-1299. doi:10.1016/j.bbabio.2010.04.019. PubMed: 20450883.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1292-1299
    • Zeth, K.1
  • 27
    • 84870013071 scopus 로고    scopus 로고
    • Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy
    • doi:10.1074/jbc.M112.419721. PubMed: 23060438
    • Sun Y, Vashisht AA, Tchieu J, Wohlschlegel JA, Dreier L (2012) Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy. J Biol Chem 287: 40652-40660. doi:10.1074/jbc.M112.419721. PubMed: 23060438.
    • (2012) J Biol Chem , vol.287 , pp. 40652-40660
    • Sun, Y.1    Vashisht, A.A.2    Tchieu, J.3    Wohlschlegel, J.A.4    Dreier, L.5
  • 28
    • 52449134572 scopus 로고    scopus 로고
    • The structure of voltage-dependent anion selective channel: State of the art
    • doi:10.1007/s10863-008-9140-3. PubMed: 18668358
    • De Pinto V, Reina S, Guarino F, Messina A (2008) The structure of Voltage-Dependent Anion selective Channel: state of the art. J Bioenerg Biomembr 40: 139-147. doi:10.1007/s10863-008-9140-3. PubMed: 18668358.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 139-147
    • De Pinto, V.1    Reina, S.2    Guarino, F.3    Messina, A.4
  • 29
    • 0026297727 scopus 로고
    • Studies on human porin VI. Production and characterization of eight monoclonal mouse antibodies against the human VDAC "porin 31HL" and their application for histotopological studies in human skeletal muscle
    • doi:10.1515/bchm3.1991.372.2.1027. PubMed: 1724155
    • Babel D, Walter G, Götz H, Thinnes FP, Jürgens L et al. (1991) Studies on human porin. VI. Production and characterization of eight monoclonal mouse antibodies against the human VDAC "Porin 31HL" and their application for histotopological studies in human skeletal muscle. Biol Chem Hoppe Seyler 372: 1027-1034. doi:10.1515/bchm3.1991.372.2.1027. PubMed: 1724155.
    • (1991) Biol Chem Hoppe Seyler , vol.372 , pp. 1027-1034
    • Babel, D.1    Walter, G.2    Götz, H.3    Thinnes, F.P.4    Jürgens, L.5
  • 30
    • 0028958295 scopus 로고
    • Immunoelectron microscopic study of the distribution of porin on outer membranes of rat heart mitochondria
    • doi:10.1007/BF02110336. PubMed: 7543088
    • Konstantinova SA, Mannella CA (1995) Immunoelectron microscopic study of the distribution of porin on outer membranes of rat heart mitochondria. J Bioenerg Biomembr 27: 93-99. doi:10.1007/BF02110336. PubMed: 7543088.
    • (1995) J Bioenerg Biomembr , vol.27 , pp. 93-99
    • Konstantinova, S.A.1    Mannella, C.A.2
  • 31
    • 0031857554 scopus 로고    scopus 로고
    • Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications
    • DOI 10.1006/jsbi.1997.3954
    • Mannella CA (1998) Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications. J Struct Biol 121: 207-218. doi:10.1006/jsbi.1997.3954. PubMed: 9615439. (Pubitemid 28361447)
    • (1998) Journal of Structural Biology , vol.121 , Issue.2 , pp. 207-218
    • Mannella, C.A.1
  • 32
    • 77953695349 scopus 로고    scopus 로고
    • Swapping of the N-terminus of VDAC1 with VDAC3 restores full activity of the channel and confers anti-aging features to the cell
    • doi:10.1016/j.febslet.2010.04.066. PubMed: 20434446
    • Reina S, Palermo V, Guarnera A, Guarino F, Messina A, et al. (2010) Swapping of the N-terminus of VDAC1 with VDAC3 restores full activity of the channel and confers anti-aging features to the cell. FEBS Lett 584: 2837-2844. doi:10.1016/j.febslet.2010.04.066. PubMed: 20434446.
    • (2010) FEBS Lett , vol.584 , pp. 2837-2844
    • Reina, S.1    Palermo, V.2    Guarnera, A.3    Guarino, F.4    Messina, A.5
  • 33
    • 35448964610 scopus 로고    scopus 로고
    • Warburg, me and hexokinase 2
    • doi:10.1007/s10863-007-9094-x. PubMed: 17879147
    • Pedersen PL (2007) Warburg, me and Hexokinase 2. J Bioenerg Biomembr 39: 211-222. doi:10.1007/s10863-007-9094-x. PubMed: 17879147.
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 211-222
    • Pedersen, P.L.1
  • 34
    • 63649100705 scopus 로고    scopus 로고
    • Voltage-dependent anion channel 1-based peptides interact with hexokinase to prevent its anti-apoptotic activity
    • PubMed: 19049977
    • Arzoine L, Zilberberg N, Ben-Romano R, Shoshan-Barmatz V (2009) Voltage-dependent anion channel 1-based peptides interact with hexokinase to prevent its anti-apoptotic activity. J Biol Chem 284: 3946-3955. PubMed: 19049977.
    • (2009) J Biol Chem , vol.284 , pp. 3946-3955
    • Arzoine, L.1    Zilberberg, N.2    Ben-Romano, R.3    Shoshan-Barmatz, V.4
  • 35
    • 79953766008 scopus 로고    scopus 로고
    • Molecular model of hexokinase binding to the outer mitochondrial membrane porin (VDAC1): Implication for the design of new cancer therapies
    • doi:10.1016/j.mito.2011.01.012. PubMed: 21315184
    • Rosano C (2011) Molecular model of hexokinase binding to the outer mitochondrial membrane porin (VDAC1): Implication for the design of new cancer therapies. Mitochondrion 11: 513-519. doi:10.1016/j.mito.2011.01.012. PubMed: 21315184.
    • (2011) Mitochondrion , vol.11 , pp. 513-519
    • Rosano, C.1
  • 36
    • 0035931765 scopus 로고    scopus 로고
    • Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells
    • DOI 10.1083/jcb.152.2.237
    • Shimizu S, Matsuoka Y, Shinohara Y, Yoneda, Tsujimoto Y (2001) Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells. J Cell Biol 152: 237-250. doi:10.1083/jcb.152.2.237. PubMed: 11266442. (Pubitemid 34285595)
    • (2001) Journal of Cell Biology , vol.152 , Issue.2 , pp. 237-250
    • Shimizu, S.1    Matsuoka, Y.2    Shinohara, Y.3    Yoneda, Y.4    Tsujimoto, Y.5
  • 37
    • 77949881804 scopus 로고    scopus 로고
    • Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity
    • doi:10.1074/jbc.M109.082990. PubMed: 20037155
    • Arbel N, Shoshan-Barmatz V (2010) Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity. J Biol Chem 285: 6053-6062. doi:10.1074/jbc.M109.082990. PubMed: 20037155.
    • (2010) J Biol Chem , vol.285 , pp. 6053-6062
    • Arbel, N.1    Shoshan-Barmatz, V.2


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