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Volumn 174, Issue 7, 2006, Pages 985-996

Cytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA

(22)  Poncet, Delphine a   Pauleau, Anne Laure a   Szabadkai, Gyorgy b   Vozza, Angelo c   Scholz, Sebastian R c   Le Bras, Morgane d   Brière, Jean Jacques e   Jalil, Abdelali f   Le Moigne, Ronan g   Brenner, Catherine d   Hahn, Gabriele h   Wittig, Ilka i   Schägger, Hermann i   Lemaire, Christophe d   Bianchi, Katiuscia b   Souquère, Sylvie j   Pierron, Gerard j   Rustin, Pierre e   Goldmacher, Victor S k   Rizzuto, Rosario b   more..

a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN VMIA; UNCLASSIFIED DRUG;

EID: 33749003497     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200604069     Document Type: Article
Times cited : (83)

References (65)
  • 2
    • 1242294492 scopus 로고    scopus 로고
    • Mechanism of actin polymerization in cellular ATP depletion
    • Atkinson, S.J., M.A. Hosford, and B.A. Molitoris. 2004. Mechanism of actin polymerization in cellular ATP depletion. J. Biol. Chem. 279:5194-5199.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5194-5199
    • Atkinson, S.J.1    Hosford, M.A.2    Molitoris, B.A.3
  • 5
    • 0035881713 scopus 로고    scopus 로고
    • Bacterial and viral proteins regulating apoptosis at the mitochondrial level
    • Boya, P., B. Roques, and G. Kroemer. 2001. Bacterial and viral proteins regulating apoptosis at the mitochondrial level. EMBO J. 20:4325-4331.
    • (2001) EMBO J. , vol.20 , pp. 4325-4331
    • Boya, P.1    Roques, B.2    Kroemer, G.3
  • 10
    • 3843147327 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome: Three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP
    • Chen, C., Y. Ko, M. Delannoy, S.J. Ludtke, W. Chiu, and P.L. Pedersen. 2004. Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. J. Biol. Chem. 279:31761-31768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31761-31768
    • Chen, C.1    Ko, Y.2    Delannoy, M.3    Ludtke, S.J.4    Chiu, W.5    Pedersen, P.L.6
  • 12
    • 0042526700 scopus 로고    scopus 로고
    • On the involvement of mitochondrial intermembrane junctional complexes in apoptosis
    • Crompton, M. 2003. On the involvement of mitochondrial intermembrane junctional complexes in apoptosis. Curr. Med. Chem. 10:1473-1484.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1473-1484
    • Crompton, M.1
  • 13
    • 0036791781 scopus 로고    scopus 로고
    • Viral homologs of BCL-2: Role of apoptosis in the regulation of virus infection
    • Cuconati, A., and E. White. 2002. Viral homologs of BCL-2: role of apoptosis in the regulation of virus infection. Genes Dev. 16:2465-2478.
    • (2002) Genes Dev. , vol.16 , pp. 2465-2478
    • Cuconati, A.1    White, E.2
  • 14
    • 0030957356 scopus 로고    scopus 로고
    • Viral manipulations of the actin cytoskeleton
    • Cudmore, S., and I. Reckmann. 1997. Viral manipulations of the actin cytoskeleton. Trends Microbiol. 5:142-148.
    • (1997) Trends Microbiol. , vol.5 , pp. 142-148
    • Cudmore, S.1    Reckmann, I.2
  • 15
    • 0033679661 scopus 로고    scopus 로고
    • Modeling ischemia in vitro: Selective depletion of adenine and guanine nucleotide pools
    • Dagher, P.C. 2000. Modeling ischemia in vitro: selective depletion of adenine and guanine nucleotide pools. Am. J. Physiol. Cell Physiol. 279:C1270-C1277.
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279
    • Dagher, P.C.1
  • 16
    • 0036890632 scopus 로고    scopus 로고
    • Central nervous system apoptosis in human herpes simplex virus and cytomegalovirus encephalitis
    • DeBiasi, R.L., B.K. Kleinschmidt-DeMasters, S. Richardson-Burns, and K.L. Tyler. 2002. Central nervous system apoptosis in human herpes simplex virus and cytomegalovirus encephalitis. J. Infect. Dis. 186:1547-1557.
    • (2002) J. Infect. Dis. , vol.186 , pp. 1547-1557
    • DeBiasi, R.L.1    Kleinschmidt-DeMasters, B.K.2    Richardson-Burns, S.3    Tyler, K.L.4
  • 18
    • 1842862375 scopus 로고    scopus 로고
    • The role of the cytoskeleton during viral infection
    • Dohner, K., and B. Sodeik. 2005. The role of the cytoskeleton during viral infection. Curr. Top. Microbiol. Immunol. 285:67-108.
    • (2005) Curr. Top. Microbiol. Immunol. , vol.285 , pp. 67-108
    • Dohner, K.1    Sodeik, B.2
  • 19
    • 0032575612 scopus 로고    scopus 로고
    • Expression in Escherichia coli, functional characterization, and tissue distribution of isoforms a and B of the phosphate carrier from bovine mitochondria
    • Fiermonte, G., V. Dolce, and F. Palmieri. 1998. Expression in Escherichia coli, functional characterization, and tissue distribution of isoforms A and B of the phosphate carrier from bovine mitochondria. J. Biol. Chem. 273:22782-22787.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22782-22787
    • Fiermonte, G.1    Dolce, V.2    Palmieri, F.3
  • 20
    • 9644259300 scopus 로고    scopus 로고
    • Human cytomegalovirus: Clinical aspects, immune regulation, and emerging treatments
    • Gandhi, M.K., and R. Khanna. 2004. Human cytomegalovirus: clinical aspects, immune regulation, and emerging treatments. Lancet Infect. Dis. 4:725-738.
    • (2004) Lancet Infect. Dis. , vol.4 , pp. 725-738
    • Gandhi, M.K.1    Khanna, R.2
  • 21
    • 85047675697 scopus 로고
    • Ischaemia and the myocyte cytoskeleton: Review and speculation
    • Ganote, C., and S. Armstrong. 1993. Ischaemia and the myocyte cytoskeleton: review and speculation. Cardiovasc. Res. 27:1387-1403.
    • (1993) Cardiovasc. Res. , vol.27 , pp. 1387-1403
    • Ganote, C.1    Armstrong, S.2
  • 22
    • 18044393021 scopus 로고    scopus 로고
    • Cell death suppression by cytomegaloviruses
    • Goldmacher, V.S. 2005. Cell death suppression by cytomegaloviruses. Apoptosis. 10:251-265.
    • (2005) Apoptosis , vol.10 , pp. 251-265
    • Goldmacher, V.S.1
  • 24
    • 0041810128 scopus 로고    scopus 로고
    • The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death
    • Halestrap, A.P., and C. Brennerb. 2003. The adenine nucleotide translocase: a central component of the mitochondrial permeability transition pore and key player in cell death. Curr. Med. Chem. 10:1507-1525.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1507-1525
    • Halestrap, A.P.1    Brennerb, C.2
  • 27
    • 0037459089 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells
    • Ishihara, N., A. Jofuku, Y. Eura, and K. Mihara. 2003. Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells. Biochem. Biophys. Res. Commun. 301:891-898.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 891-898
    • Ishihara, N.1    Jofuku, A.2    Eura, Y.3    Mihara, K.4
  • 28
    • 0022762880 scopus 로고
    • Cytoskeletal disruption during human cytomegalovirus infection of human lung fibroblasts
    • Jones, N.L., J.C. Lewis, and B.A. Kilpatrick. 1986. Cytoskeletal disruption during human cytomegalovirus infection of human lung fibroblasts. Eur. J. Cell Biol. 41:304-312.
    • (1986) Eur. J. Cell Biol. , vol.41 , pp. 304-312
    • Jones, N.L.1    Lewis, J.C.2    Kilpatrick, B.A.3
  • 29
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
    • Jouaville, L.S., P. Pinton, C. Bastianutto, G.A. Rutter, and R. Rizzuto. 1999. Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming. Proc. Natl. Acad. Sci. USA. 96:13807-13812.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13807-13812
    • Jouaville, L.S.1    Pinton, P.2    Bastianutto, C.3    Rutter, G.A.4    Rizzuto, R.5
  • 31
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R.M., E. Bossy-Wetzel, D.R. Green, and D.D. Newmeyer. 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275:1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 32
    • 0027978726 scopus 로고
    • Productive infection of human endometrial stromal cells by human cytomegalovirus
    • Kowalik, T.F., A.D. Yurochko, C.A. Rinehart, C.V. Lee, and E.S. Huang. 1994. Productive infection of human endometrial stromal cells by human cytomegalovirus. Virology. 202:247-257.
    • (1994) Virology , vol.202 , pp. 247-257
    • Kowalik, T.F.1    Yurochko, A.D.2    Rinehart, C.A.3    Lee, C.V.4    Huang, E.S.5
  • 33
    • 0036906665 scopus 로고    scopus 로고
    • Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins
    • Legros, F., A. Lombes, P. Frachon, and M. Rojo. 2002. Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins. Mol. Biol. Cell. 13:4343-4354.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4343-4354
    • Legros, F.1    Lombes, A.2    Frachon, P.3    Rojo, M.4
  • 34
    • 14644441669 scopus 로고    scopus 로고
    • Newcomers in the process of mitochondrial permeabilization
    • Lucken-Ardjomande, S., and J.C. Martinou. 2005. Newcomers in the process of mitochondrial permeabilization. J. Cell Sci. 118:473-483.[
    • (2005) J. Cell Sci. , vol.118 , pp. 473-483
    • Lucken-Ardjomande, S.1    Martinou, J.C.2
  • 35
    • 33744930897 scopus 로고    scopus 로고
    • Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells
    • Machida, K., Y. Ohta, and H. Osada. 2006. Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells. J. Biol. Chem. 281:14314-14320.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14314-14320
    • Machida, K.1    Ohta, Y.2    Osada, H.3
  • 37
    • 0037213306 scopus 로고    scopus 로고
    • Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis
    • McCormick, A.L., V.L. Smith, D. Chow, and E.S. Mocarski. 2003. Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis. J. Virol. 77:631-641.
    • (2003) J. Virol. , vol.77 , pp. 631-641
    • McCormick, A.L.1    Smith, V.L.2    Chow, D.3    Mocarski, E.S.4
  • 38
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan, A., C.L. Smith, I. Lamensdorf, S.H. Yoon, and R.J. Youle. 2001. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 153:1265-1276.
    • (2001) J. Cell Biol. , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 39
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): Physiological and pathological implications
    • Palmieri, F. 2004. The mitochondrial transporter family (SLC25): physiological and pathological implications. Pflugers Arch. 447:689-709.
    • (2004) Pflugers Arch. , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 40
    • 0018337987 scopus 로고
    • Direct methods for measuring metabolite transport and distribution in mitochondria
    • Palmieri, F., and M. Klingenberg. 1979. Direct methods for measuring metabolite transport and distribution in mitochondria. Methods Enzymol. 56:279-301.
    • (1979) Methods Enzymol. , vol.56 , pp. 279-301
    • Palmieri, F.1    Klingenberg, M.2
  • 41
    • 0034693854 scopus 로고    scopus 로고
    • Focal adhesion kinase: A regulator of focal adhesion dynamics and cell movement
    • Parsons, J.T., K.H. Martin, J.K. Slack, J.M. Taylor, and S.A. Weed. 2000. Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement. Oncogene. 19:5606-5613.
    • (2000) Oncogene , vol.19 , pp. 5606-5613
    • Parsons, J.T.1    Martin, K.H.2    Slack, J.K.3    Taylor, J.M.4    Weed, S.A.5
  • 42
    • 0023724881 scopus 로고
    • Increase in the ADP/ATP exchange in rat liver mitochondria irradiated in vitro by helium-neon laser
    • Passarella, S., A. Ostuni, A. Atlante, and E. Quagliariello. 1988. Increase in the ADP/ATP exchange in rat liver mitochondria irradiated in vitro by helium-neon laser. Biochem. Biophys. Res. Commun. 156 (2):978-986.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , Issue.2 , pp. 978-986
    • Passarella, S.1    Ostuni, A.2    Atlante, A.3    Quagliariello, E.4
  • 44
    • 16844377411 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in the control of apoptosis
    • Perfettini, J.-L., T. Roumier, and G. Kroemer. 2005. Mitochondrial fusion and fission in the control of apoptosis. Trends Cell Biol. 15:179-183.
    • (2005) Trends Cell Biol. , vol.15 , pp. 179-183
    • Perfettini, J.-L.1    Roumier, T.2    Kroemer, G.3
  • 45
    • 0035144435 scopus 로고    scopus 로고
    • Viral transport and the cytoskeleton
    • Ploubidou, A., and M. Way. 2001. Viral transport and the cytoskeleton. Curr. Opin. Cell Biol. 13:97-105.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 97-105
    • Ploubidou, A.1    Way, M.2
  • 47
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou, M., and A. Hall. 2004. Cell migration: Rho GTPases lead the way. Dev. Biol. 265:23-32.
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 48
    • 9944262385 scopus 로고    scopus 로고
    • Human cytomegalovirus proteins encoded by UL37 exon 1 protect infected fibroblasts against virus-induced apoptosis and are required for efficient virus replication
    • Reboredo, M., R.F. Greaves, and G. Hahn. 2004. Human cytomegalovirus proteins encoded by UL37 exon 1 protect infected fibroblasts against virus-induced apoptosis and are required for efficient virus replication. J. Gen. Virol. 85:3555-3567.
    • (2004) J. Gen. Virol. , vol.85 , pp. 3555-3567
    • Reboredo, M.1    Greaves, R.F.2    Hahn, G.3
  • 49
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley, A.J. 2001. Rho GTPases and cell migration. J. Cell Sci. 114:2713-2722.
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 53
    • 2942748250 scopus 로고    scopus 로고
    • Identification of cytomegalovirus in a liquid-based gynecologic sample using morphology, immunohistochemistry, and DNA real-time PCR detection
    • Sekhon, H.S., R.D. Press, W.A. Schmidt, M. Hawley, and A. Rader. 2004. Identification of cytomegalovirus in a liquid-based gynecologic sample using morphology, immunohistochemistry, and DNA real-time PCR detection. Diagn. Cytopathol. 30:411-417.
    • (2004) Diagn. Cytopathol. , vol.30 , pp. 411-417
    • Sekhon, H.S.1    Press, R.D.2    Schmidt, W.A.3    Hawley, M.4    Rader, A.5
  • 54
    • 0036838778 scopus 로고    scopus 로고
    • Site-specific alteration of actin assembly visualized in living renal epithelial cells during ATP depletion
    • Shelden, E.A., J.M. Weinberg, D.R. Sorenson, C.A. Edwards, and F.M. Pollock. 2002. Site-specific alteration of actin assembly visualized in living renal epithelial cells during ATP depletion. J. Am. Soc. Nephrol. 13:2667-2680.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2667-2680
    • Shelden, E.A.1    Weinberg, J.M.2    Sorenson, D.R.3    Edwards, C.A.4    Pollock, F.M.5
  • 55
    • 0030979562 scopus 로고    scopus 로고
    • Disordered migration and loss of virus-infected neuronal cells in developing mouse brains infected with murine cytomegalovirus
    • Shinmura, Y., I. Kosugi, S. Aiba-Masago, S. Baba, L.R. Yong, and Y. Tsutsui. 1997. Disordered migration and loss of virus-infected neuronal cells in developing mouse brains infected with murine cytomegalovirus. Acta Neuropathol. (Berl.). 93:551-557.
    • (1997) Acta Neuropathol. (Berl.) , vol.93 , pp. 551-557
    • Shinmura, Y.1    Kosugi, I.2    Aiba-Masago, S.3    Baba, S.4    Yong, L.R.5    Tsutsui, Y.6
  • 57
    • 0043198196 scopus 로고    scopus 로고
    • Detection of apoptoses in gastrointestinal graft-versus-host disease and cytomegalovirus colitis by a commercially available antibody against caspase-3
    • Tzankov, A., G. Stifter, I. Tschorner, G. Gastl, and G. Mikuz. 2003. Detection of apoptoses in gastrointestinal graft-versus-host disease and cytomegalovirus colitis by a commercially available antibody against caspase-3. Pathol. Res. Pract. 199:337-340.
    • (2003) Pathol. Res. Pract. , vol.199 , pp. 337-340
    • Tzankov, A.1    Stifter, G.2    Tschorner, I.3    Gastl, G.4    Mikuz, G.5
  • 58
    • 0032587982 scopus 로고    scopus 로고
    • Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange
    • Vander Heiden, M.G., N.S. Chandel, P.T. Schumacker, and C.B. Thompson. 1999. Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. Mol. Cell. 3:159-167.
    • (1999) Mol. Cell , vol.3 , pp. 159-167
    • Vander Heiden, M.G.1    Chandel, N.S.2    Schumacker, P.T.3    Thompson, C.B.4
  • 59
    • 0035380462 scopus 로고    scopus 로고
    • Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane
    • Vander Heiden, M.G., X.X. Li, E. Gottleib, R.B. Hill, C.B. Thompson, and M. Colombini. 2001. Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane. J. Biol. Chem. 276:19414-19419.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19414-19419
    • Vander Heiden, M.G.1    Li, X.X.2    Gottleib, E.3    Hill, R.B.4    Thompson, C.B.5    Colombini, M.6
  • 61
    • 0028670859 scopus 로고
    • Down-regulation of integrin alpha 1/beta 1 expression and association with cell rounding in human cytomegalovirus-infected fibroblasts
    • Warren, A.P., C.N. Owens, L.K. Borysiewicz, and K. Patel. 1994. Down-regulation of integrin alpha 1/beta 1 expression and association with cell rounding in human cytomegalovirus-infected fibroblasts. J. Gen. Virol. 75:3319-3325.
    • (1994) J. Gen. Virol. , vol.75 , pp. 3319-3325
    • Warren, A.P.1    Owens, C.N.2    Borysiewicz, L.K.3    Patel, K.4
  • 64
    • 0034602188 scopus 로고    scopus 로고
    • Role of BAX in the apoptotic response to anticancer agents
    • Zhang, L., J. Yu, B.H. Park, K.W. Kinzler, and B. Vogelstein. 2000. Role of BAX in the apoptotic response to anticancer agents. Science. 290:989-992.
    • (2000) Science , vol.290 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3    Kinzler, K.W.4    Vogelstein, B.5
  • 65
    • 0029760303 scopus 로고    scopus 로고
    • Bcl-2 mutants with restricted subcellular localization reveal spatially distinct pathways for apoptosis in different cell types
    • Zhu, W., A. Cowie, G.W. Wasfy, L.Z. Penn, B. Leber, and D.W. Andrews. 1996. Bcl-2 mutants with restricted subcellular localization reveal spatially distinct pathways for apoptosis in different cell types. EMBO J. 15:4130-4141.
    • (1996) EMBO J. , vol.15 , pp. 4130-4141
    • Zhu, W.1    Cowie, A.2    Wasfy, G.W.3    Penn, L.Z.4    Leber, B.5    Andrews, D.W.6


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