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Volumn 425, Issue 3, 2010, Pages 567-573

FLIM-FRET and FRAP reveal association of influenza virus haemagglutinin with membrane rafts

Author keywords

Budding; Fluorescent imaging; Haemagglutinin; Palmitoylation; Raft; Transmembrane region

Indexed keywords

BIOPHYSICAL METHODS; CHINESE HAMSTER OVARY; CYAN FLUORESCENT PROTEIN; CYTOPLASMIC TAIL; FLIM-FRET; FLUORESCENCE LIFETIME IMAGING MICROSCOPY; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; FLUORESCENT IMAGING; GLYCOSYLATED; INFLUENZA VIRUS; INNER LEAFLETS; LIVING CELL; MEMBRANE FUSION; PALMITOYLATION; PLASMA MEMBRANES; RESONANCE ENERGY TRANSFER; TRANSMEMBRANE REGIONS; VIRUS BUDDING; YELLOW FLUORESCENT PROTEINS;

EID: 74349083523     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20091388     Document Type: Article
Times cited : (74)

References (40)
  • 1
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin, M. (2003) The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32, 257-283
    • (2003) Annu. Rev. Biophys. Biomol. Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 2
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • Jacobson, K., Mouritsen, O. G. and Anderson, R. G. (2007) Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9, 7-14
    • (2007) Nat. Cell Biol , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.3
  • 3
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: Scale-dependent, active lipid organization at the cell surface
    • Mayor, S. and Rao, M. (2004) Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 5, 231-240
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 5
    • 1842482773 scopus 로고    scopus 로고
    • Model systems, lipid rafts, and cell membranes
    • Simons, K. and Vaz, W. L. (2004) Model systems, lipid rafts, and cell membranes. Annu. Rev. Biophys. Biomol. Struct. 33, 269-295
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 269-295
    • Simons, K.1    Vaz, W.L.2
  • 6
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositolanchored protein at the apical surface of MDCK cells examined at a resolution of < 100 ° using imaging fluorescence resonance energy transfer
    • Kenworthy, A. K. and Edidin, M. (1998) Distribution of a glycosylphosphatidylinositolanchored protein at the apical surface of MDCK cells examined at a resolution of < 100 ° using imaging fluorescence resonance energy transfer. J. Cell Biol. 142, 69-84
    • (1998) J. Cell Biol , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 7
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy, A. K., Petranova, N. and Edidin, M. (2000) High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell 11, 1645-1655
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 8
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov, O. O. and Nichols, B. J. (2004) Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat. Cell Biol. 6, 238-243
    • (2004) Nat. Cell Biol , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 10
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D. A., Violin, J. D., Newton, A. C. and Tsien, R. Y. (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 11
    • 0027257099 scopus 로고
    • Glycosphingolipidenriched, detergent-insoluble complexes in protein sorting in epithelial cells
    • Fiedler, K., Kobayashi, T., Kurzchalia, T. V. and Simons, K. (1993) Glycosphingolipidenriched, detergent-insoluble complexes in protein sorting in epithelial cells. Biochemistry 32, 6365-6373
    • (1993) Biochemistry , vol.32 , pp. 6365-6373
    • Fiedler, K.1    Kobayashi, T.2    Kurzchalia, T.V.3    Simons, K.4
  • 12
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., Roth, M. G. and Simons, K. (1997) Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16, 5501-5508
    • (1997) EMBO J , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 13
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian, K. A., Ostermeyer, A. G., Chen, J. Z., Roth, M. G. and Brown, D. A. (1999) Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274, 3910-3917
    • (1999) J. Biol. Chem , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 14
    • 0024547523 scopus 로고
    • Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens, J. E., Roth, M. G. and Matlin, K. S. (1989) Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol. 108, 821-832
    • (1989) J. Cell Biol , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 15
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K. and van Meer, G. (1988) Lipid sorting in epithelial cells. Biochemistry 27, 6197-6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    van Meer, G.2
  • 16
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., Rietveld, A., Wilk, T. and Simons, K. (1999) Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274, 2038-2044
    • (1999) J. Biol. Chem , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 17
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda, M., Leser, G. P., Russell, C. J. and Lamb, R. A. (2003) Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc. Natl. Acad. Sci. U.S.A. 100, 14610-14617
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 18
    • 34547656276 scopus 로고    scopus 로고
    • The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts
    • Wang, X., Hinson, E. R. and Cresswell, P. (2007) The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts. Cell Host Microbe 2, 96-105
    • (2007) Cell Host Microbe , vol.2 , pp. 96-105
    • Wang, X.1    Hinson, E.R.2    Cresswell, P.3
  • 19
    • 0345599000 scopus 로고    scopus 로고
    • Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts
    • Shvartsman, D. E., Kotler, M., Tall, R. D., Roth, M. G. and Henis, Y. I. (2003) Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts. J. Cell Biol. 163, 879-888
    • (2003) J. Cell Biol , vol.163 , pp. 879-888
    • Shvartsman, D.E.1    Kotler, M.2    Tall, R.D.3    Roth, M.G.4    Henis, Y.I.5
  • 21
    • 22344442585 scopus 로고    scopus 로고
    • Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin
    • Hess, S. T., Kumar, M., Verma, A., Farrington, J., Kenworthy, A. and Zimmerberg, J. (2005) Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin. J. Cell Biol. 169, 965-976
    • (2005) J. Cell Biol , vol.169 , pp. 965-976
    • Hess, S.T.1    Kumar, M.2    Verma, A.3    Farrington, J.4    Kenworthy, A.5    Zimmerberg, J.6
  • 22
    • 36849053761 scopus 로고    scopus 로고
    • Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories
    • Hess, S. T., Gould, T. J., Gudheti, M. V., Maas, S. A., Mills, K. D. and Zimmerberg, J. (2007) Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories. Proc. Natl. Acad. Sci. U.S.A. 104, 17370-17375
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 17370-17375
    • Hess, S.T.1    Gould, T.J.2    Gudheti, M.V.3    Maas, S.A.4    Mills, K.D.5    Zimmerberg, J.6
  • 23
    • 27644440465 scopus 로고    scopus 로고
    • Influenza virus assembly and budding in raft-derived microdomains: A quantitative analysis of the surface distribution of HA, NA and M2 proteins
    • Leser, G. P. and Lamb, R. A. (2005) Influenza virus assembly and budding in raft-derived microdomains: a quantitative analysis of the surface distribution of HA, NA and M2 proteins. Virology 342, 215-227
    • (2005) Virology , vol.342 , pp. 215-227
    • Leser, G.P.1    Lamb, R.A.2
  • 24
    • 67650103574 scopus 로고    scopus 로고
    • Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging
    • Scolari, S., Engel, S., Krebs, N., Plazzo, A. P., De Almeida, R. F., Prieto, M., Veit, M. and Herrmann, A. (2009) Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging. J. Biol. Chem. 284, 15708-15716
    • (2009) J. Biol. Chem , vol.284 , pp. 15708-15716
    • Scolari, S.1    Engel, S.2    Krebs, N.3    Plazzo, A.P.4    De Almeida, R.F.5    Prieto, M.6    Veit, M.7    Herrmann, A.8
  • 25
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • Rizzo, M. A., Springer, G. H., Granada, B. and Piston, D. W. (2004) An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22, 445-449
    • (2004) Nat. Biotechnol , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 26
    • 0026748702 scopus 로고
    • Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R
    • Vey, M., Orlich, M., Adler, S., Klenk, H. D., Rott, R. and Garten, W. (1992) Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R. Virology 188, 408-413
    • (1992) Virology , vol.188 , pp. 408-413
    • Vey, M.1    Orlich, M.2    Adler, S.3    Klenk, H.D.4    Rott, R.5    Garten, W.6
  • 27
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
    • Veit, M., Kretzschmar, E., Kuroda, K., Garten, W., Schmidt, M. F., Klenk, H. D. and Rott, R. (1991) Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin. J. Virol. 65, 2491-2500
    • (1991) J. Virol , vol.65 , pp. 2491-2500
    • Veit, M.1    Kretzschmar, E.2    Kuroda, K.3    Garten, W.4    Schmidt, M.F.5    Klenk, H.D.6    Rott, R.7
  • 29
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., Koppel, D. E., Schlessinger, J., Elson, E. and Webb, W. W. (1976) Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16, 1055-1069
    • (1976) Biophys. J , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 30
    • 0028130488 scopus 로고
    • Lateral mobility of tetramethylrhodamine (TMR) labelled G protein a and β? subunits in NG 108-15 cells
    • Kwon, G., Axelrod, D. and Neubig, R. R. (1994) Lateral mobility of tetramethylrhodamine (TMR) labelled G protein a and β? subunits in NG 108-15 cells. Cell. Signalling 6, 663-679
    • (1994) Cell. Signalling , vol.6 , pp. 663-679
    • Kwon, G.1    Axelrod, D.2    Neubig, R.R.3
  • 31
    • 0020197884 scopus 로고
    • Lateral mobility in membranes as detected by fluorescence recovery after photobleaching
    • Yguerabide, J., Schmidt, J. A. and Yguerabide, E. E. (1982) Lateral mobility in membranes as detected by fluorescence recovery after photobleaching. Biophys. J. 40, 69-75
    • (1982) Biophys. J , vol.40 , pp. 69-75
    • Yguerabide, J.1    Schmidt, J.A.2    Yguerabide, E.E.3
  • 32
    • 0028081894 scopus 로고
    • Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein
    • Ohuchi, M., Cramer, A., Vey, M., Ohuchi, R., Garten, W. and Klenk, H. D. (1994) Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein. J. Virol. 68, 920-926
    • (1994) J. Virol , vol.68 , pp. 920-926
    • Ohuchi, M.1    Cramer, A.2    Vey, M.3    Ohuchi, R.4    Garten, W.5    Klenk, H.D.6
  • 33
    • 0028177960 scopus 로고
    • Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transport
    • Takeuchi, K. and Lamb, R. A. (1994) Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transport. J. Virol. 68, 911-919
    • (1994) J. Virol , vol.68 , pp. 911-919
    • Takeuchi, K.1    Lamb, R.A.2
  • 34
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe, H. and Periasamy, A. (2005) Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16, 19-27
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 35
    • 33645275730 scopus 로고    scopus 로고
    • Fluorescence-quenching and resonance energy transfer studies of lipid microdomains in model and biological membranes
    • Silvius, J. R. and Nabi, I. R. (2006) Fluorescence-quenching and resonance energy transfer studies of lipid microdomains in model and biological membranes. Mol. Membr. Biol. 23, 5-16
    • (2006) Mol. Membr. Biol , vol.23 , pp. 5-16
    • Silvius, J.R.1    Nabi, I.R.2
  • 36
    • 0023006195 scopus 로고
    • Assembly of influenza hemagglutinin trimers and its role in intracellular transport
    • Copeland, C. S., Doms, R. W., Bolzau, E. M., Webster, R. G. and Helenius, A. (1986) Assembly of influenza hemagglutinin trimers and its role in intracellular transport. J. Cell Biol. 103, 1179-1191
    • (1986) J. Cell Biol , vol.103 , pp. 1179-1191
    • Copeland, C.S.1    Doms, R.W.2    Bolzau, E.M.3    Webster, R.G.4    Helenius, A.5
  • 38
    • 31044439024 scopus 로고    scopus 로고
    • Phase coexistence and connectivity in the apical membrane of polarized epithelial cells
    • Meder, D., Moreno, M. J., Verkade, P., Vaz, W. L. and Simons, K. (2006) Phase coexistence and connectivity in the apical membrane of polarized epithelial cells. Proc. Natl. Acad. Sci. U.S.A. 103, 329-334
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 329-334
    • Meder, D.1    Moreno, M.J.2    Verkade, P.3    Vaz, W.L.4    Simons, K.5
  • 39
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle, A., Keller, P., Florin, E. L., Simons, K. and Horber, J. K. (2000) Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell Biol. 148, 997-1008
    • (2000) J. Cell Biol , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 40
    • 39549095341 scopus 로고    scopus 로고
    • Mechanisms for enveloped virus budding: Can some viruses do without an ESCRT?
    • Chen, B. J. and Lamb, R. A. (2008) Mechanisms for enveloped virus budding: can some viruses do without an ESCRT? Virology 372, 221-232
    • (2008) Virology , vol.372 , pp. 221-232
    • Chen, B.J.1    Lamb, R.A.2


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