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Volumn 116, Issue 16, 2003, Pages 3433-3442

Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8

Author keywords

Cytoskeleton; Retroviris; Spumavirus; Trafficking

Indexed keywords

AMINO ACID; CELL PROTEIN; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; GAG PROTEIN; RECOMBINANT DNA;

EID: 0041384017     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00613     Document Type: Review
Times cited : (106)

References (55)
  • 2
    • 0034170083 scopus 로고    scopus 로고
    • Toward a more accurate quantitation of the activity of recombinant retroviruses: Alternatives to titer and multiplicity of infection
    • Andreadis, S., Lavery, T., Davis, H. E., Le Doux, J. M., Yarmush, M. L. and Morgan, J. R. (2000). Toward a more accurate quantitation of the activity of recombinant retroviruses: alternatives to titer and multiplicity of infection. J. Virol. 74, 1258-1266.
    • (2000) J. Virol. , vol.74 , pp. 1258-1266
    • Andreadis, S.1    Lavery, T.2    Davis, H.E.3    Le Doux, J.M.4    Yarmush, M.L.5    Morgan, J.R.6
  • 3
    • 0030861056 scopus 로고    scopus 로고
    • Dimerization of the highly conserved light chain shared by dynein and myosin V
    • Benashski, S. E., Harrison, A., Patel-King, R. S. and King, S. M. (1997). Dimerization of the highly conserved light chain shared by dynein and myosin V. J. Biol. Chem. 272, 20929-20935.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20929-20935
    • Benashski, S.E.1    Harrison, A.2    Patel-King, R.S.3    King, S.M.4
  • 4
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J. K., Echeverri, C. J., Nilsson, T. and Vallee, R. B. (1997). Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139, 469-484.
    • (1997) J. Cell Biol. , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 5
    • 0032560079 scopus 로고    scopus 로고
    • Dynein and dynactin are localized to astral microtubules and at cortical sites in mitotic epithelial cells
    • Busson, S., Dujardin, D., Moreau, A., Dompierre, J. and De Mey, J. R. (1998). Dynein and dynactin are localized to astral microtubules and at cortical sites in mitotic epithelial cells. Curr. Biol. 8, 541-544.
    • (1998) Curr. Biol. , vol.8 , pp. 541-544
    • Busson, S.1    Dujardin, D.2    Moreau, A.3    Dompierre, J.4    De Mey, J.R.5
  • 6
    • 0030613781 scopus 로고    scopus 로고
    • I kappa B alpha physically interacts with a cytoskeleton-associated protein through its signal response domain
    • Crepieux, P., Kwon, H., Leclerc, N., Spencer, W., Richard, S., Lin, R. and Hiscott, J. (1997). I kappa B alpha physically interacts with a cytoskeleton-associated protein through its signal response domain. Mol. Cell. Biol. 17, 7375-7385.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7375-7385
    • Crepieux, P.1    Kwon, H.2    Leclerc, N.3    Spencer, W.4    Richard, S.5    Lin, R.6    Hiscott, J.7
  • 8
    • 0032407404 scopus 로고    scopus 로고
    • Intracellular pathogens and the actin cytoskeleton
    • Dramsi, S. and Cossart, P. (1998). Intracellular pathogens and the actin cytoskeleton. Annu. Rev. Cell. Dev. Biol. 14, 137-166.
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 137-166
    • Dramsi, S.1    Cossart, P.2
  • 9
    • 0034947737 scopus 로고    scopus 로고
    • Identification of a conserved residue of foamy virus Gag required for intracellular capsid assembly
    • Eastman, S. W. and Linial, M. L. (2001). Identification of a conserved residue of foamy virus Gag required for intracellular capsid assembly. J. Virol. 75, 6857-6864.
    • (2001) J. Virol. , vol.75 , pp. 6857-6864
    • Eastman, S.W.1    Linial, M.L.2
  • 12
    • 0035182168 scopus 로고    scopus 로고
    • Surfing pathogens and the lessons learned for actin polymerization
    • Frischknecht, F. and Way, M. (2001). Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol. 11, 30-38.
    • (2001) Trends Cell Biol. , vol.11 , pp. 30-38
    • Frischknecht, F.1    Way, M.2
  • 14
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata, R., Bebok, Z., Sorscher, E. J. and Sztul, E. S. (1999). Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol. 146, 1239-1254.
    • (1999) J. Cell Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 15
    • 0034772321 scopus 로고    scopus 로고
    • Movements of vaccinia virus intracellular enveloped virions with GFP tagged to the F13L envelope protein
    • Geada, M. M., Galindo, I., Lorenzo, M. M., Perdiguero, B. and Blasco, R. (2001). Movements of vaccinia virus intracellular enveloped virions with GFP tagged to the F13L envelope protein. J. Gen. Virol. 82, 2747-2760.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2747-2760
    • Geada, M.M.1    Galindo, I.2    Lorenzo, M.M.3    Perdiguero, B.4    Blasco, R.5
  • 16
    • 0031027096 scopus 로고    scopus 로고
    • Expression and maturation of human foamy virus Gag precursor polypeptides
    • Giron, M. L., Colas, S., Wybier, J., Rozain, F. and Emanoil-Ravier, R. (1997). Expression and maturation of human foamy virus Gag precursor polypeptides. J. Virol. 71, 1635-1639.
    • (1997) J. Virol. , vol.71 , pp. 1635-1639
    • Giron, M.L.1    Colas, S.2    Wybier, J.3    Rozain, F.4    Emanoil-Ravier, R.5
  • 17
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • Goode, B. L., Drubin, D. G. and Barnes, G. (2000). Functional cooperation between the microtubule and actin cytoskeletons. Curr. Opin. Cell Biol. 12, 63-71.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 19
    • 0035972239 scopus 로고    scopus 로고
    • Aggresomes resemble sites specialized for virus assembly
    • Heath, C. M., Windsor, M. and Wileman, T. (2001). Aggresomes resemble sites specialized for virus assembly. J. Cell Biol. 153, 449-455.
    • (2001) J. Cell Biol. , vol.153 , pp. 449-455
    • Heath, C.M.1    Windsor, M.2    Wileman, T.3
  • 21
    • 0033775766 scopus 로고    scopus 로고
    • Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
    • Jacob, Y., Badrane, H., Ceccaldi, P. E. and Tordo, N. (2000). Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. J. Virol. 74, 10217-10222.
    • (2000) J. Virol. , vol.74 , pp. 10217-10222
    • Jacob, Y.1    Badrane, H.2    Ceccaldi, P.E.3    Tordo, N.4
  • 22
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey, S. R. and Snyder, S. H. (1996). PIN: an associated protein inhibitor of neuronal nitric oxide synthase. Science 274, 774-777.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 23
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J. A., Ward, C. L. and Kopito, R. R. (1998). Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 24
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S. and Holzbaur, E. L. (1999). Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell. Biol. 11, 45-53.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 25
    • 0026562720 scopus 로고
    • Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene
    • Kimpton, J. and Emerman, M. (1992). Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene. J. Virol. 66, 2232-2239.
    • (1992) J. Virol. , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 26
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. (2000). Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 27
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (KR)XTQT motif
    • Lo, K. W., Naisbitt, S., Fan, J. S., Sbeng, M. and Zhang, M. (2001). The 8-kDa dynein light chain binds to its targets via a conserved (KR)XTQT motif. J. Biol. Chem. 276, 14059-14066.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14059-14066
    • Lo, K.W.1    Naisbitt, S.2    Fan, J.S.3    Sbeng, M.4    Zhang, M.5
  • 30
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt, S., Valtschanoff, J., Allison, D. W., Sala, C., Kim, E., Craig, A. M., Weinberg, R. J. and Sheng, M. (2000). Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein J. Neurosci. 20, 4524-4534.
    • (2000) J. Neurosci. , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Craig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 31
    • 0034091334 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 entry into host cells: Reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro
    • Ojala, P. M., Sodeik, B., Ebersold, M. W., Kutay, U. and Helenius, A. (2000). Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol. Cell. Biol. 20, 4922-4931.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 4922-4931
    • Ojala, P.M.1    Sodeik, B.2    Ebersold, M.W.3    Kutay, U.4    Helenius, A.5
  • 32
    • 0020309907 scopus 로고
    • Purification and polypeptide composition of dynein ATPases from Chlamydomonas flagella
    • Pfister, K. K., Fay, R. B. and Witman, G. B. (1982). Purification and polypeptide composition of dynein ATPases from Chlamydomonas flagella. Cell Motil. 2, 525-547.
    • (1982) Cell Motil. , vol.2 , pp. 525-547
    • Pfister, K.K.1    Fay, R.B.2    Witman, G.B.3
  • 35
    • 0018332854 scopus 로고
    • Axonemal adenosine triphosphatases from flagella of Chlamydomonas reinhardtii. Purification of two dyneins
    • Piperno, G. and Luck, D. J. (1979). Axonemal adenosine triphosphatases from flagella of Chlamydomonas reinhardtii. Purification of two dyneins. J. Biol. Chem. 254, 3084-3090.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3084-3090
    • Piperno, G.1    Luck, D.J.2
  • 36
    • 0035144435 scopus 로고    scopus 로고
    • Viral transport and the cytoskeleton
    • Ploubidou, A. and Way, M. (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
  • 37
    • 0034254776 scopus 로고    scopus 로고
    • Vaccinia virus infection disrupts microtubule organization and centrosome function
    • Ploubidou, A., Moreau, V., Ashman, K., Reckmann, I., Gonzalez, C. and Way, M. (2000). Vaccinia virus infection disrupts microtubule organization and centrosome function. EMBO J. 19, 3932-3944.
    • (2000) EMBO J. , vol.19 , pp. 3932-3944
    • Ploubidou, A.1    Moreau, V.2    Ashman, K.3    Reckmann, I.4    Gonzalez, C.5    Way, M.6
  • 38
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath, H., Villunger, A., O'Reilly, L. A., Beaumont, J. G., Coultas, L., Cheney, R. E., Huang, D. C. and Strasser, A. (2001). Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 293, 1829-1832.
    • (2001) Science , vol.293 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.7    Strasser, A.8
  • 40
    • 0033776043 scopus 로고    scopus 로고
    • Interaction of the rabies virus P protein with the LC8 dynein light chain
    • Raux, H., Flamand, A. and Blondel, D. (2000). Interaction of the rabies virus P protein with the LC8 dynein light chain. J. Virol. 74, 10212-10216.
    • (2000) J. Virol. , vol.74 , pp. 10212-10216
    • Raux, H.1    Flamand, A.2    Blondel, D.3
  • 42
    • 0035903004 scopus 로고    scopus 로고
    • Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique
    • Rodriguez-Crespo, I., Yelamos, B., Roncal, F., Albar, J. P., Ortiz de Montellano, P. R. and Gavilanes, F. (2001). Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique. FEBS Lett. 503, 135-141.
    • (2001) FEBS Lett. , vol.503 , pp. 135-141
    • Rodriguez-Crespo, I.1    Yelamos, B.2    Roncal, F.3    Albar, J.P.4    Ortiz de Montellano, P.R.5    Gavilanes, F.6
  • 43
    • 1842404827 scopus 로고    scopus 로고
    • Nuclear targeting of incoming human foamy virus Gag proteins involves a centriolar step
    • Saib, A., Puvion-Dutilleul, F., Schmid, M., Peries, J. and de The, H. (1997). Nuclear targeting of incoming human foamy virus Gag proteins involves a centriolar step. J. Virol. 71, 1155-1161.
    • (1997) J. Virol. , vol.71 , pp. 1155-1161
    • Saib, A.1    Puvion-Dutilleul, F.2    Schmid, M.3    Peries, J.4    de The, H.5
  • 44
    • 0037059618 scopus 로고    scopus 로고
    • Cytoplasmic dynein as a facilitator of nuclear envelope breakdown
    • Salina, D., Bodoor, K., Eckley, M. D., Schroer, T. A., Rattner, J. B. and Burke, B. (2002). Cytoplasmic dynein as a facilitator of nuclear envelope breakdown. Cell 108, 97-107.
    • (2002) Cell , vol.108 , pp. 97-107
    • Salina, D.1    Bodoor, K.2    Eckley, M.D.3    Schroer, T.A.4    Rattner, J.B.5    Burke, B.6
  • 45
    • 0028338650 scopus 로고
    • Nuclear localization of foamy virus Gag precursor protein
    • Schliephake, A. W. and Rethwilm, A. (1994). Nuclear localization of foamy virus Gag precursor protein. J. Virol. 68, 4946-4954.
    • (1994) J. Virol. , vol.68 , pp. 4946-4954
    • Schliephake, A.W.1    Rethwilm, A.2
  • 46
    • 0034307164 scopus 로고    scopus 로고
    • Mechanisms of viral transport in the cytoplasm
    • Sodeik, B. (2000). Mechanisms of viral transport in the cytoplasm. Trends Microbiol. 8, 465-472.
    • (2000) Trends Microbiol. , vol.8 , pp. 465-472
    • Sodeik, B.1
  • 47
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik, B., Ebersold, M. W. and Helenius, A. (1997). Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 136, 1007-1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 48
    • 0031005278 scopus 로고    scopus 로고
    • Researchers in cell motility and the cytoskeleton can play major roles in understanding AIDS
    • Soll, D. R. (1997). Researchers in cell motility and the cytoskeleton can play major roles in understanding AIDS. Cell Motil. Cytoskeleton 37, 91-97.
    • (1997) Cell Motil. Cytoskeleton , vol.37 , pp. 91-97
    • Soll, D.R.1
  • 49
    • 0033593811 scopus 로고    scopus 로고
    • Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus
    • Suomalainen, M., Nakano, M. Y., Keller, S., Boucke, K., Stidwill, R. P. and Greber, U. F. (1999). Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. J. Cell Biol. 144, 657-672.
    • (1999) J. Cell Biol. , vol.144 , pp. 657-672
    • Suomalainen, M.1    Nakano, M.Y.2    Keller, S.3    Boucke, K.4    Stidwill, R.P.5    Greber, U.F.6
  • 51
    • 0035050188 scopus 로고    scopus 로고
    • Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag
    • Tobaly-Tapiero, J., Bittoun, P., Giron, M. L., Neves, M., Koken, M., de The, H. and Saib, A. (2001). Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag. J. Virol. 75, 4367-4375.
    • (2001) J. Virol. , vol.75 , pp. 4367-4375
    • Tobaly-Tapiero, J.1    Bittoun, P.2    Giron, M.L.3    Neves, M.4    Koken, M.5    de The, H.6    Saib, A.7
  • 52
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1
    • Trotman, L. C., Mosberger, N., Fornerod, M., Stidwill, R. P. and Greber, U. F. (2001). Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1 . Nat. Cell Biol. 3, 1092-1100.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1092-1100
    • Trotman, L.C.1    Mosberger, N.2    Fornerod, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 54
    • 0035164017 scopus 로고    scopus 로고
    • Vaccinia virus intracellular movement is associated with microtubules and independent of actin tails
    • Ward, B. M. and Moss, B. (2001). Vaccinia virus intracellular movement is associated with microtubules and independent of actin tails. J. Virol. 75, 11651-11663.
    • (2001) J. Virol. , vol.75 , pp. 11651-11663
    • Ward, B.M.1    Moss, B.2
  • 55
    • 0029864543 scopus 로고    scopus 로고
    • The carboxyl terminus of the human foamy virus Gag protein contains separable nucleic acid binding and nuclear transport domains
    • Yu, S. F., Edelmann, K., Strong, R. K., Moebes, A., Rethwilm, A. and Linial, M. L. (1996). The carboxyl terminus of the human foamy virus Gag protein contains separable nucleic acid binding and nuclear transport domains. J. Virol. 70, 8255-8262.
    • (1996) J. Virol. , vol.70 , pp. 8255-8262
    • Yu, S.F.1    Edelmann, K.2    Strong, R.K.3    Moebes, A.4    Rethwilm, A.5    Linial, M.L.6


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