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Volumn 228, Issue 2, 1997, Pages 285-293

High concentration of the EBV latent membrane protein 1 in glycosphingolipid-rich complexes from both epithelial and lymphoid cells

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSPHINGOLIPID; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; VIRUS PROTEIN;

EID: 0031575514     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.8380     Document Type: Article
Times cited : (47)

References (44)
  • 1
    • 0024503782 scopus 로고
    • The multiple membrane-spanning segments of the BNLF-1 oncogene from Epstein-Barr virus are required for transformation
    • Baichwal V. R., Sugden B. The multiple membrane-spanning segments of the BNLF-1 oncogene from Epstein-Barr virus are required for transformation. Oncogene. 4:1989;67-74.
    • (1989) Oncogene , vol.4 , pp. 67-74
    • Baichwal, V.R.1    Sugden, B.2
  • 2
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D. A., Rose J. K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell. 68:1992;533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 5
    • 0028113411 scopus 로고
    • Signal transduction of a G protein-coupled receptor in caveolae: Colocalization of endothelin and its receptor with caveolin
    • Chun M., Liyanage U. K., Lisanti M. P., Lodish H. F. Signal transduction of a G protein-coupled receptor in caveolae: Colocalization of endothelin and its receptor with caveolin. Proc. Natl. Acad. Sci. USA. 91:1994;11728-11732.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11728-11732
    • Chun, M.1    Liyanage, U.K.2    Lisanti, M.P.3    Lodish, H.F.4
  • 6
    • 0025271424 scopus 로고
    • Epstein-Barr virus latent membrane protein inhibits human epithelial cell differentiation
    • Dawson C. W., Rickinson A. B., Young L. S. Epstein-Barr virus latent membrane protein inhibits human epithelial cell differentiation. Nature. 344:1990;777-780.
    • (1990) Nature , vol.344 , pp. 777-780
    • Dawson, C.W.1    Rickinson, A.B.2    Young, L.S.3
  • 7
    • 0029994378 scopus 로고    scopus 로고
    • Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases
    • Deckert M., Ticchioni M., Bernard A. Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases. J. Cell. Biol. 133:1996;791-799.
    • (1996) J. Cell. Biol. , vol.133 , pp. 791-799
    • Deckert, M.1    Ticchioni, M.2    Bernard, A.3
  • 8
    • 0026524220 scopus 로고
    • Correlation of the expression of Epstein-Barr virus latent membrane protein and in situ hybridization with biotinylated BamH1-W probes in Hodgkin's disease
    • Delsol G., Brousset P., Chittal S., Rigual-Huguet F. Correlation of the expression of Epstein-Barr virus latent membrane protein and in situ hybridization with biotinylated BamH1-W probes in Hodgkin's disease. Am. J. Pathol. 140:1992;247-253.
    • (1992) Am. J. Pathol. , vol.140 , pp. 247-253
    • Delsol, G.1    Brousset, P.2    Chittal, S.3    Rigual-Huguet, F.4
  • 10
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra A. M., Williamson E., Simons K., Parton R. G. Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J. Biol. Chem. 269:1994;30745-30748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 11
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21- caveolin
    • Fra A. M., Williamson E., Simons K., Parton R. G. De novo formation of caveolae in lymphocytes by expression of VIP21- caveolin. Proc. Natl. Acad. Sci. USA. 92:1995;8655-8659.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 12
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent- resistant complexes without caveolin
    • Gorodinsky A., Harris D. A. Glycolipid-anchored proteins in neuroblastoma cells form detergent- resistant complexes without caveolin. J. Cell Biol. 129:1995;619-627.
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 13
    • 0026700212 scopus 로고
    • Epstein-Barr virus latent membrane protein transactivates the human immunodeficiency virus type 1 long terminal repeat through induction of NF-kappa B activity
    • Hammarskjold M. L., Simurda M. C. Epstein-Barr virus latent membrane protein transactivates the human immunodeficiency virus type 1 long terminal repeat through induction of NF-kappa B activity. J. Virol. 66:1992;6496-6501.
    • (1992) J. Virol. , vol.66 , pp. 6496-6501
    • Hammarskjold, M.L.1    Simurda, M.C.2
  • 14
    • 0028947029 scopus 로고
    • Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes
    • Hanada K., Nishijima M., Akamatsu Y., Pagano R. E. Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes. J. Biol. Chem. 270:1995;6254-6260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6254-6260
    • Hanada, K.1    Nishijima, M.2    Akamatsu, Y.3    Pagano, R.E.4
  • 15
    • 0027215533 scopus 로고
    • Clonability and tumorigenicity of human epithelial cells expressing the EBV encoded membrane protein LMP1
    • Hu L. F., Chen F., Zheng X., Ernberg I., Cao S. L., Christensson B., Klein G., Winberg G. Clonability and tumorigenicity of human epithelial cells expressing the EBV encoded membrane protein LMP1. Oncogene. 8:1993;1575-1583.
    • (1993) Oncogene , vol.8 , pp. 1575-1583
    • Hu, L.F.1    Chen, F.2    Zheng, X.3    Ernberg, I.4    Cao, S.L.5    Christensson, B.6    Klein, G.7    Winberg, G.8
  • 16
    • 0028853402 scopus 로고
    • The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NF-kappa B and cell surface phenotype via two effector regions in its carboxy-terminal cytoplasmic domain
    • Huen D. S., Henderson S. A., Croom-Carter D., Rowe M. The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NF-kappa B and cell surface phenotype via two effector regions in its carboxy-terminal cytoplasmic domain. Oncogene. 10:1995;549-560.
    • (1995) Oncogene , vol.10 , pp. 549-560
    • Huen, D.S.1    Henderson, S.A.2    Croom-Carter, D.3    Rowe, M.4
  • 17
    • 0004250834 scopus 로고    scopus 로고
    • Philadelphia/New York: Lippincott-Raven. p. 2343-2396
    • Kieff E. Fields Virology. 1996;Lippincott-Raven, Philadelphia/New York. p. 2343-2396.
    • (1996) Fields Virology
    • Kieff, E.1
  • 18
    • 0028953271 scopus 로고
    • Reduction of caveolin and caveolae in oncogenically transformed cells
    • Koleske A. J., Baltimore D., Lisanti M. P. Reduction of caveolin and caveolae in oncogenically transformed cells. Proc. Natl. Acad. Sci. USA. 92:1995;1381-1385.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1381-1385
    • Koleske, A.J.1    Baltimore, D.2    Lisanti, M.P.3
  • 19
    • 0028933450 scopus 로고
    • Guilt by insolubility - Does a protein's detergent insolubility reflect a caveolar location?
    • Kurzchalia T. V., Hartmann E., Dupree P. Guilt by insolubility - Does a protein's detergent insolubility reflect a caveolar location? Trends Cell Biol. 5:1995;187-189.
    • (1995) Trends Cell Biol. , vol.5 , pp. 187-189
    • Kurzchalia, T.V.1    Hartmann, E.2    Dupree, P.3
  • 20
    • 0022501165 scopus 로고
    • Orientation and patching of the latent infection membrane protein encoded by Epstein-Barr virus
    • Liebowitz D., Wang D., Kieff E. Orientation and patching of the latent infection membrane protein encoded by Epstein-Barr virus. J. Virol. 58:1986;233-237.
    • (1986) J. Virol. , vol.58 , pp. 233-237
    • Liebowitz, D.1    Wang, D.2    Kieff, E.3
  • 21
    • 0023369137 scopus 로고
    • An Epstein-Barr virus transforming protein associates with vimentin in lymphocytes
    • Liebowitz D., Kopan R., Fuchs E., Sample J., Kieff E. An Epstein-Barr virus transforming protein associates with vimentin in lymphocytes. Mol. Cell Biol. 7:1987;2299-2308.
    • (1987) Mol. Cell Biol. , vol.7 , pp. 2299-2308
    • Liebowitz, D.1    Kopan, R.2    Fuchs, E.3    Sample, J.4    Kieff, E.5
  • 22
    • 0024307672 scopus 로고
    • Epstein-Barr virus latent membrane protein: Induction of B-cell activation antigens and membrane patch formation does not require vimentin
    • Liebowitz D., Kieff E. Epstein-Barr virus latent membrane protein: Induction of B-cell activation antigens and membrane patch formation does not require vimentin. J. Virol. 63:1989;4051-4054.
    • (1989) J. Virol. , vol.63 , pp. 4051-4054
    • Liebowitz, D.1    Kieff, E.2
  • 23
    • 0022217534 scopus 로고
    • Epstein-Barr virus-encoded protein found in plasma membranes of transformed cells
    • Mann K. P., Staunton D., Thorley-Lawson D. A. Epstein-Barr virus-encoded protein found in plasma membranes of transformed cells. J. Virol. 55:1985;710-720.
    • (1985) J. Virol. , vol.55 , pp. 710-720
    • Mann, K.P.1    Staunton, D.2    Thorley-Lawson, D.A.3
  • 24
    • 0023230360 scopus 로고
    • Posttranslational processing of the Epstein-Barr virus-encoded p63/LMP protein
    • Mann K. P., Thorley-Lawson D. Posttranslational processing of the Epstein-Barr virus-encoded p63/LMP protein. J. Virol. 61:1987;2100-2108.
    • (1987) J. Virol. , vol.61 , pp. 2100-2108
    • Mann, K.P.1    Thorley-Lawson, D.2
  • 25
    • 0026264856 scopus 로고
    • The latent membrane protein oncoprotein resembles growth factor receptors in the properties of its turnover
    • Martin J., Sugden B. The latent membrane protein oncoprotein resembles growth factor receptors in the properties of its turnover. Cell Growth. Differ. 2:1991a;653-660.
    • (1991) Cell Growth. Differ. , vol.2 , pp. 653-660
    • Martin, J.1    Sugden, B.2
  • 26
    • 0026042281 scopus 로고
    • Transformation by the oncogenic latent membrane protein correlates with its rapid turnover, membrane localization, and cytoskeletal association
    • Martin J., Sugden B. Transformation by the oncogenic latent membrane protein correlates with its rapid turnover, membrane localization, and cytoskeletal association. J. Virol. 65:1991b;3246-3258.
    • (1991) J. Virol. , vol.65 , pp. 3246-3258
    • Martin, J.1    Sugden, B.2
  • 27
    • 0029063936 scopus 로고
    • The Epstein-Barr virus latent membrane protein 1 induces expression of the epidermal growth factor receptor
    • Miller W. E., Earp H. S., Raab-Traub N. The Epstein-Barr virus latent membrane protein 1 induces expression of the epidermal growth factor receptor. J. Virol. 69:1995;4390-4398.
    • (1995) J. Virol. , vol.69 , pp. 4390-4398
    • Miller, W.E.1    Earp, H.S.2    Raab-Traub, N.3
  • 28
    • 0028987479 scopus 로고
    • Stimulation of NF-kappa B-mediated transcription by mutant derivatives of the latent membrane protein of Epstein-Barr virus
    • Mitchell T., Sugden B. Stimulation of NF-kappa B-mediated transcription by mutant derivatives of the latent membrane protein of Epstein-Barr virus. J. Virol. 69:1995;2968-2976.
    • (1995) J. Virol. , vol.69 , pp. 2968-2976
    • Mitchell, T.1    Sugden, B.2
  • 29
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C., Kieff E. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell. 80:1995;389-399.
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1    Birkenbach, M.2    Yalamanchili, R.3    Vanarsdale, T.4    Ware, C.5    Kieff, E.6
  • 32
    • 0029037660 scopus 로고
    • Expression of LMP1 in epithelial cells leads to the activation of a select subset of NF-kappa B/Rel family proteins
    • Paine E., Scheinman R. I., Baldwin A. S., Raab-Traub N. Expression of LMP1 in epithelial cells leads to the activation of a select subset of NF-kappa B/Rel family proteins. J. Virol. 69:1995;4572-4576.
    • (1995) J. Virol. , vol.69 , pp. 4572-4576
    • Paine, E.1    Scheinman, R.I.2    Baldwin, A.S.3    Raab-Traub, N.4
  • 33
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton R. G. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42:1994;155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 34
    • 0029051898 scopus 로고
    • Clonal proliferations of cells infected with Epstein-Barr virus in preinvasive lesions related to nasopharyngeal carcinoma
    • Pathmanathan R., Prasad U., Sadler R., Flynn K., Raab-Traub N. Clonal proliferations of cells infected with Epstein-Barr virus in preinvasive lesions related to nasopharyngeal carcinoma. N. Engl. J. Med. 333:1995;693-698.
    • (1995) N. Engl. J. Med. , vol.333 , pp. 693-698
    • Pathmanathan, R.1    Prasad, U.2    Sadler, R.3    Flynn, K.4    Raab-Traub, N.5
  • 35
    • 0004250834 scopus 로고    scopus 로고
    • B.N. Fields, D.M. Knipe, P.M. Howley, R.M. Chanock, J.L. Melnick, T.P. Monath, B. Roizman, & S.E. Straus. Philadelphia/New York: Lippincott-Raven
    • Rickinson A. B., Kieff E. Fields B. N., Knipe D. M., Howley P. M., Chanock R. M., Melnick J. L., Monath T. P., Roizman B., Straus S. E. Fields Virology. 1996;2397-2446 Lippincott-Raven, Philadelphia/New York.
    • (1996) Fields Virology , pp. 2397-2446
    • Rickinson, A.B.1    Kieff, E.2
  • 37
    • 0023244909 scopus 로고
    • Monoclonal antibodies to the latent membrane protein of Epstein-Barr virus reveal heterogeneity of the protein and inducible expression in virus-transformed cells
    • Rowe M., Evans H. S., Young L. S., Hennessy K., Kieff E., Rickinson A. B. Monoclonal antibodies to the latent membrane protein of Epstein-Barr virus reveal heterogeneity of the protein and inducible expression in virus-transformed cells. J. Gen. Virol. 68:1987;1575-1586.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1575-1586
    • Rowe, M.1    Evans, H.S.2    Young, L.S.3    Hennessy, K.4    Kieff, E.5    Rickinson, A.B.6
  • 38
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M., Sudol M., Tang Z., Lisanti M. P. Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 122:1993;789-807.
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 40
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer J. E., McIntosh D. P., Dvorak A. M., Liu J., Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science. 269:1995;1435-1439.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 41
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder R., London E., Brown D. Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc. Natl. Acad. Sci. USA. 91:1994;12130-12134.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 42
    • 0028842801 scopus 로고
    • Exogenous glycosyl phosphatidylinositol-anchored CD 59 associates with kinases in membrane clusters on U937 cells and becomes Ca+-signaling competent
    • Van Den Berg C. W., Cinek T., Hallett M. B., Horejsi V., Morgan B. P. Exogenous glycosyl phosphatidylinositol-anchored CD 59 associates with kinases in membrane clusters on U937 cells and becomes Ca+-signaling competent. J. Cell. Biol. 131:1995;669-677.
    • (1995) J. Cell. Biol. , vol.131 , pp. 669-677
    • Van Den Berg, C.W.1    Cinek, T.2    Hallett, M.B.3    Horejsi, V.4    Morgan, B.P.5
  • 43
    • 0022309824 scopus 로고
    • An EBV membrane protein expressed in immortalized lymphocytes transforms established rodent cells
    • Wang D., Liebowitz D., Kieff E. An EBV membrane protein expressed in immortalized lymphocytes transforms established rodent cells. Cell. 43:1985;831-840.
    • (1985) Cell , vol.43 , pp. 831-840
    • Wang, D.1    Liebowitz, D.2    Kieff, E.3
  • 44
    • 0025342480 scopus 로고
    • Epstein-Barr virus latent membrane protein (LMP1) and nuclear proteins 2 and 3C are effectors of phenotypic changes in B lymphocytes: EBNA-2 and LMP1 cooperatively induce CD23
    • Wang F., Gregory C., Sample C., Rowe M., Liebowitz D., Murray R., Rickinson A., Kieff E. Epstein-Barr virus latent membrane protein (LMP1) and nuclear proteins 2 and 3C are effectors of phenotypic changes in B lymphocytes: EBNA-2 and LMP1 cooperatively induce CD23. J. Virol. 64:1990;2309-2318.
    • (1990) J. Virol. , vol.64 , pp. 2309-2318
    • Wang, F.1    Gregory, C.2    Sample, C.3    Rowe, M.4    Liebowitz, D.5    Murray, R.6    Rickinson, A.7    Kieff, E.8


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