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Volumn 10, Issue 8, 2014, Pages 2134-2145

Live cell interactome of the human voltage dependent anion channel 3 (VDAC3) revealed in HeLa cells by affinity purification tag technique

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PROTEOME; VDAC3 PROTEIN, HUMAN; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 84903781999     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/c4mb00237g     Document Type: Article
Times cited : (23)

References (49)
  • 1
    • 0018847077 scopus 로고
    • Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane
    • M. Colombini Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane Ann. N. Y. Acad. Sci. 1980 341 552 563
    • (1980) Ann. N. Y. Acad. Sci. , vol.341 , pp. 552-563
    • Colombini, M.1
  • 3
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function
    • T. Rostovtseva M. Colombini VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function Biophys. J. 1997 72 1954 1962
    • (1997) Biophys. J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 4
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial Membrane Permeabilization in Cell Death
    • G. Kroemer L. Galluzzi C. Brenner Mitochondrial Membrane Permeabilization in Cell Death Physiol. Rev. 2007 87 99 163
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 5
    • 71749121777 scopus 로고    scopus 로고
    • Et al., Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo durings stress-induced apoptosis
    • F. Tomasello A. Messina L. Lartigue L. Schembri C. Medina S. Reina et al., Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo durings stress-induced apoptosis Cell Res. 2009 19 1363 1376
    • (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
  • 8
    • 0027930089 scopus 로고
    • Deficiency of the Voltage-Dependent Anion Channel (VDAC): A novel cause of mitochondrial myopathies
    • M. Huizing W. Ruitenbeek F. Thinnes V. De Pinto Deficiency of the Voltage-Dependent Anion Channel (VDAC): a novel cause of mitochondrial myopathies Lancet 1994 344 762
    • (1994) Lancet , vol.344 , pp. 762
    • Huizing, M.1    Ruitenbeek, W.2    Thinnes, F.3    De Pinto, V.4
  • 9
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • S. Hiller R. G. Garces T. J. Malia V. Y. Orekhov M. Colombini G. Wagner Solution structure of the integral human membrane protein VDAC-1 in detergent micelles Science 2008 321 1206 1210
    • (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
  • 11
    • 56649099192 scopus 로고    scopus 로고
    • Et al., the crystal structure of mouse VDAC1 at 2.3 angstrom resolution reveals mechanistic insights into metabolite gating
    • R. Ujwal D. Cascio J. P. Colletier S. Faham J. Zhang et al., The crystal structure of mouse VDAC1 at 2.3 angstrom resolution reveals mechanistic insights into metabolite gating Proc. Natl. Acad. Sci. U. S. A. 2008 105 17742 17747
    • (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
  • 12
    • 52449134572 scopus 로고    scopus 로고
    • The structure of Voltage-Dependent Anion selective Channel: State of the art
    • V. De Pinto S. Reina F. Guarino A. Messina The structure of Voltage-Dependent Anion selective Channel: state of the art J. Bioenerg. Biomembr. 2008 40 139 147
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 139-147
    • De Pinto, V.1    Reina, S.2    Guarino, F.3    Messina, A.4
  • 13
    • 84891905707 scopus 로고    scopus 로고
    • The Voltage-Dependent Anion selective Channel 1 (VDAC1) topography in the mitochondrial outer membrane as detected in intact cell
    • F. M. Tomasello F. Guarino A. Messina S. Reina V. De Pinto The Voltage-Dependent Anion selective Channel 1 (VDAC1) topography in the mitochondrial outer membrane as detected in intact cell PLoS One 2013 8 e81522
    • (2013) PLoS One , vol.8 , pp. 81522
    • Tomasello, F.M.1    Guarino, F.2    Messina, A.3    Reina, S.4    De Pinto, V.5
  • 16
    • 0032765963 scopus 로고    scopus 로고
    • Mouse VDAC isoforms expressed in yeast: Channel properties and their roles in mitochondrial outer membrane permeability
    • X. Xu W. Decker M. J. Sampson W. J. Craigen M. Colombini Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability J. Membr. Biol. 1999 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
  • 17
    • 77953695349 scopus 로고    scopus 로고
    • Et al., Swapping of the N-terminus of VDAC1 with VDAC3 restores full activity of the channel and confers anti-aging features to the cell
    • S. Reina V. Palermo F. Guarino A. Messina C. Mazzoni et al., 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. 2010 584 2837 2844
    • (2010) FEBS Lett. , vol.584 , pp. 2837-2844
    • Reina, S.1    Palermo, V.2    Guarino, F.3    Messina, A.4    Mazzoni, C.5
  • 20
    • 84867275965 scopus 로고    scopus 로고
    • VDAC3 regulates centriole assembly by targeting Mps1 to centrosomes
    • S. Majumder M. Slabodnick A. Pike J. Marquardt H. A. Fisk VDAC3 regulates centriole assembly by targeting Mps1 to centrosomes Cell Cycle 2012 11 3666 3678
    • (2012) Cell Cycle , vol.11 , pp. 3666-3678
    • Majumder, S.1    Slabodnick, M.2    Pike, A.3    Marquardt, J.4    Fisk, H.A.5
  • 21
    • 2442468057 scopus 로고    scopus 로고
    • Voltage-dependent anion selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers a cytoskeletal component of the sperm flagellum
    • K. D. Hinsch V. De Pinto V. A. Aires X. Schneider A. Messina E. Hinsch Voltage-dependent anion selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers a cytoskeletal component of the sperm flagellum J. Biol. Chem. 2004 279 15281 15288
    • (2004) J. Biol. Chem. , vol.279 , pp. 15281-15288
    • Hinsch, K.D.1    De Pinto, V.2    Aires, V.A.3    Schneider, X.4    Messina, A.5    Hinsch, E.6
  • 22
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • G. Rigaut A. Shevchenko B. Rutz M. Wilm M. Mann B. Séraphin A generic protein purification method for protein complex characterization and proteome exploration Nat. Biotechnol. 1999 17 1030 1032
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6
  • 23
    • 0033549555 scopus 로고    scopus 로고
    • A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein
    • M. M. Rolls P. A. Stein S. S. Taylor E. Ha F. McKeon T. A. Rapoport A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein J. Cell Biol. 1999 146 29 42
    • (1999) J. Cell Biol. , vol.146 , pp. 29-42
    • Rolls, M.M.1    Stein, P.A.2    Taylor, S.S.3    Ha, E.4    McKeon, F.5    Rapoport, T.A.6
  • 24
    • 0032544921 scopus 로고    scopus 로고
    • Development of a bicistronic vector driven by the human polypeptide chain elongation factor 1alpha promoter for creation of stable mammalian cell lines that express very high levels of recombinant proteins
    • S. Hobbs S. Jitrapakdee J. C. Wallace Development of a bicistronic vector driven by the human polypeptide chain elongation factor 1alpha promoter for creation of stable mammalian cell lines that express very high levels of recombinant proteins Biochem. Biophys. Res. Commun. 1998 252 368 372
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 368-372
    • Hobbs, S.1    Jitrapakdee, S.2    Wallace, J.C.3
  • 25
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • A. Shevchenko M. Wilm O. Vorm M. Mann Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 1996 68 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 26
    • 0035897190 scopus 로고    scopus 로고
    • VDAC2 (porin-2) expression pattern and localization in the bovine testis
    • K. D. Hinsch Asmarinah E. Hinsch L. Konrad VDAC2 (porin-2) expression pattern and localization in the bovine testis Biochim. Biophys. Acta 2001 1518 329 333
    • (2001) Biochim. Biophys. Acta , vol.1518 , pp. 329-333
    • Hinsch, K.D.1    Asmarinah2    Hinsch, E.3    Konrad, L.4
  • 27
    • 84890224333 scopus 로고    scopus 로고
    • A comprehensive strategy to identify stoichiometric membrane protein interactomes
    • A. Gokhale P. Perez-Cornejo C. Duran H. C. Hartzell V. Faundez A comprehensive strategy to identify stoichiometric membrane protein interactomes Cell Logist. 2012 2 189 196
    • (2012) Cell Logist. , vol.2 , pp. 189-196
    • Gokhale, A.1    Perez-Cornejo, P.2    Duran, C.3    Hartzell, H.C.4    Faundez, V.5
  • 28
    • 33749238923 scopus 로고    scopus 로고
    • Hunting interactomes of a membrane protein: Obtaining the largest set of voltage-dependent anion channel-interacting protein epitopes
    • I. Roman J. Figys G. Steurs M. Zizi Hunting interactomes of a membrane protein: obtaining the largest set of voltage-dependent anion channel-interacting protein epitopes Mol. Cell. Proteomics 2006 5 1667 1680
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1667-1680
    • Roman, I.1    Figys, J.2    Steurs, G.3    Zizi, M.4
  • 30
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM)
    • A. Raturi T. Simmen Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM) Biochim. Biophys. Acta 2013 1833 213 224
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 31
    • 84873248602 scopus 로고    scopus 로고
    • In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM)
    • C. N. Poston S. C. Krishnan C. R. Bazemore-Walker In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM) J. Proteomics 2013 79 219 230
    • (2013) J. Proteomics , vol.79 , pp. 219-230
    • Poston, C.N.1    Krishnan, S.C.2    Bazemore-Walker, C.R.3
  • 33
    • 79960716413 scopus 로고    scopus 로고
    • Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
    • M. Karbowski R. J. Youle Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation Curr. Opin. Cell Biol. 2011 23 476 482
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 476-482
    • Karbowski, M.1    Youle, R.J.2
  • 37
    • 79551663809 scopus 로고    scopus 로고
    • The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
    • S. Xu G. Peng Y. Wang S. Fang M. Karbowski The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover Mol. Biol. Cell 2011 22 291 300
    • (2011) Mol. Biol. Cell , vol.22 , pp. 291-300
    • Xu, S.1    Peng, G.2    Wang, Y.3    Fang, S.4    Karbowski, M.5
  • 38
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during unfolded protein response
    • B. Bernales K. L. McDonald P. Walter Autophagy counterbalances endoplasmic reticulum expansion during unfolded protein response PLoS Biol. 2006 4 e423
    • (2006) PLoS Biol. , vol.4 , pp. 423
    • Bernales, B.1    McDonald, K.L.2    Walter, P.3
  • 40
    • 84859742434 scopus 로고    scopus 로고
    • VDAC inhibition by tubulin and its physiological implications
    • T. K. Rostovtseva S. M. Bezrukov VDAC inhibition by tubulin and its physiological implications Biochim. Biophys. Acta 2012 1818 1526 1535
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1526-1535
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 42
    • 84874627577 scopus 로고    scopus 로고
    • VDAC3 and Mps1 negatively regulate ciliogenesis
    • S. Majumder H. A. Fisk VDAC3 and Mps1 negatively regulate ciliogenesis Cell Cycle 2013 12 849 858
    • (2013) Cell Cycle , vol.12 , pp. 849-858
    • Majumder, S.1    Fisk, H.A.2
  • 43
    • 33947219266 scopus 로고    scopus 로고
    • Et al., Large-scale mapping of human protein-protein interactions by mass spectrometry
    • R. M. Ewing P. Chu F. Elisma H. Li et al., Large-scale mapping of human protein-protein interactions by mass spectrometry Mol. Syst. Biol. 2007 3 89
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 89
    • Ewing, R.M.1    Chu, P.2    Elisma, F.3    Li, H.4
  • 44
    • 84892575903 scopus 로고    scopus 로고
    • Redox regulation of mitochondrial function with enphasis on cysteine oxidation reactions
    • R. J. Mailloux X. Jin W. G. Willmore Redox regulation of mitochondrial function with enphasis on cysteine oxidation reactions Redox Biol. 2014 2 123 139
    • (2014) Redox Biol. , vol.2 , pp. 123-139
    • Mailloux, R.J.1    Jin, X.2    Willmore, W.G.3
  • 45
    • 0342905085 scopus 로고    scopus 로고
    • Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel, HVDAC3, and alters its transmembrane potential
    • Z. Rahmani K. W. Huh R. Lasher A. Siddiqui Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel, HVDAC3, and alters its transmembrane potential J. Virol. 2000 74 2840 2846
    • (2000) J. Virol. , vol.74 , pp. 2840-2846
    • Rahmani, Z.1    Huh, K.W.2    Lasher, R.3    Siddiqui, A.4
  • 46
    • 0036257364 scopus 로고    scopus 로고
    • Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74
    • C. Schwarzer S. Barnikol-Watanabe F. P. Thinnes N. Hilschmann Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74 Int. J. Biochem. Cell Biol. 2002 34 1059 1070
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1059-1070
    • Schwarzer, C.1    Barnikol-Watanabe, S.2    Thinnes, F.P.3    Hilschmann, N.4
  • 47
    • 84870013071 scopus 로고    scopus 로고
    • Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy
    • Y. Sun A. A. Vashisht J. Tchieu J. A. Wohlschlegel L. Dreier Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy J. Biol. Chem. 2012 287 40652 40660
    • (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
  • 48
    • 84879896693 scopus 로고    scopus 로고
    • Et al., the mitochondrial Italian Human Proteome Project initiative (mt-HPP)
    • A. Urbani et al., The mitochondrial Italian Human Proteome Project initiative (mt-HPP) Mol. Biosyst. 2013 8 1984 1992
    • (2013) Mol. Biosyst. , vol.8 , pp. 1984-1992
    • Urbani, A.1


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