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Volumn 105, Issue 21, 2008, Pages 7405-7409

Biochemical visualization of cell surface molecular clustering in living cells

Author keywords

Ganglioside; Integrin; Microdomain; Radicals

Indexed keywords

BETA1 INTEGRIN; GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE; ANTIBODY; ENZYME; MEMBRANE PROTEIN;

EID: 44949097310     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0710346105     Document Type: Article
Times cited : (136)

References (32)
  • 1
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • Jacobson K, Mouritsen OG, Anderson RG (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
  • 2
    • 0038492661 scopus 로고    scopus 로고
    • Dynamic, yet structured: The cell membrane three decades after the Singer-Nicolson model
    • Vereb G, et al. (2003) Dynamic, yet structured: The cell membrane three decades after the Singer-Nicolson model. Proc Natl Acad Sci USA 100:8053-8058.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8053-8058
    • Vereb, G.1
  • 3
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E (1998) Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 4
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass AD, Vale RD (2005) Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121:937-950.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 5
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 6
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 7
    • 0033970146 scopus 로고    scopus 로고
    • Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques
    • Fancy DA (2000) Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques. Curr Opin Chem Biol 4:28-33.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 28-33
    • Fancy, D.A.1
  • 8
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner J (1993) New photolabeling and crosslinking methods. Annu Rev Biochem 62:483-514.
    • (1993) Annu Rev Biochem , vol.62 , pp. 483-514
    • Brunner, J.1
  • 9
    • 0017338248 scopus 로고
    • Chemical cross-linking: Reagents and problems in studies of membrane structure
    • Peters K, Richards F (1977) Chemical cross-linking: reagents and problems in studies of membrane structure. Annu Rev Biochem 46:523-551.
    • (1977) Annu Rev Biochem , vol.46 , pp. 523-551
    • Peters, K.1    Richards, F.2
  • 10
    • 0033792318 scopus 로고    scopus 로고
    • Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles
    • Thiele C, Hannah MJ, Fahrenholz F, Huttner WB (2000) Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles. Nat Cell Biol 2:42-49.
    • (2000) Nat Cell Biol , vol.2 , pp. 42-49
    • Thiele, C.1    Hannah, M.J.2    Fahrenholz, F.3    Huttner, W.B.4
  • 11
    • 0037874731 scopus 로고    scopus 로고
    • Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • Schütz G, Kada G, Pastushenko V, Schindler H (2000) Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy. EMBO J 19:892-901.
    • (2000) EMBO J , vol.19 , pp. 892-901
    • Schütz, G.1    Kada, G.2    Pastushenko, V.3    Schindler, H.4
  • 12
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako Y, Minoghchi S, Yanagida T (2000) Single-molecule imaging of EGFR signalling on the surface of living cells. Nat Cell Biol 2:168-172.
    • (2000) Nat Cell Biol , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 13
    • 0034995774 scopus 로고    scopus 로고
    • Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface
    • Iino R, Koyama I, Kusumi A (2001) Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface. Biophys J 80:2667-2677.
    • (2001) Biophys J , vol.80 , pp. 2667-2677
    • Iino, R.1    Koyama, I.2    Kusumi, A.3
  • 14
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
    • Kusumi A, Sako Y, Yamamoto M (1993) Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells. Biophys J 65:2021-2040.
    • (1993) Biophys J , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 15
    • 0026528045 scopus 로고
    • Tracking of cell surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera. Low-density lipoprotein and influenza virus receptor mobility at 4 degrees C
    • Anderson C, Georgiou G, Morrison I, Stevenson G, Cherry R (1992) Tracking of cell surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera. Low-density lipoprotein and influenza virus receptor mobility at 4 degrees C. J Cell Sci 101 (Pt 2):415-425.
    • (1992) J Cell Sci , vol.101 , Issue.PART 2 , pp. 415-425
    • Anderson, C.1    Georgiou, G.2    Morrison, I.3    Stevenson, G.4    Cherry, R.5
  • 16
    • 0029162080 scopus 로고
    • Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis
    • Simson R, Sheets E, Jacobson K (1995) Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis. Biophys J 69:989-993.
    • (1995) Biophys J , vol.69 , pp. 989-993
    • Simson, R.1    Sheets, E.2    Jacobson, K.3
  • 17
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S (1998) GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 18
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Å using imaging fluorescence resonance energy transfer
    • Kenworthy A, Edidin M (1998) Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Å using imaging fluorescence resonance energy transfer. J Cell Biol 142:69-84.
    • (1998) J Cell Biol , vol.142 , pp. 69-84
    • Kenworthy, A.1    Edidin, M.2
  • 19
    • 0000601644 scopus 로고
    • Selective destruction of protein function by chromophore-assisted laser inactivation
    • Jay DG (1988) Selective destruction of protein function by chromophore-assisted laser inactivation. Proc Natl Acad Sci USA 85:5454-5458.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5454-5458
    • Jay, D.G.1
  • 20
    • 0036203661 scopus 로고    scopus 로고
    • Fluorophore-assisted light inactivation: A high-throughput tool for direct target validation of proteins
    • Beck S, et al. (2002) Fluorophore-assisted light inactivation: a high-throughput tool for direct target validation of proteins. Proteomics 2:247-255.
    • (2002) Proteomics , vol.2 , pp. 247-255
    • Beck, S.1
  • 21
    • 0028333737 scopus 로고
    • Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals
    • Liao JC, Roider J, Jay DG (1994) Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals. Proc Natl Acad Sci USA 91:2659-2663.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2659-2663
    • Liao, J.C.1    Roider, J.2    Jay, D.G.3
  • 22
    • 0032516015 scopus 로고    scopus 로고
    • Chromophore-assisted light inactivation and self-organization of microtubules and motors
    • Surrey T, et al. (1998) Chromophore-assisted light inactivation and self-organization of microtubules and motors. Proc Natl Acad Sci USA 95:4293-4298.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4293-4298
    • Surrey, T.1
  • 23
    • 0026848362 scopus 로고
    • Quenching of singlet oxygen by biomolecules from L1210 leukemia cells
    • Baker A, Kanofsky JR (1992) Quenching of singlet oxygen by biomolecules from L1210 leukemia cells. Photochem Photobiol 55:523-528.
    • (1992) Photochem Photobiol , vol.55 , pp. 523-528
    • Baker, A.1    Kanofsky, J.R.2
  • 24
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets ED, Lee GM, Simson R, Jacobson K (1997) Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane. Biochemistry 36:12449-12458.
    • (1997) Biochemistry , vol.36 , pp. 12449-12458
    • Sheets, E.D.1    Lee, G.M.2    Simson, R.3    Jacobson, K.4
  • 25
    • 0028243194 scopus 로고
    • Compartmentalized structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis
    • Sako Y, Kusumi A (1994) Compartmentalized structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis. J Cell Biol 125:1251-1264.
    • (1994) J Cell Biol , vol.125 , pp. 1251-1264
    • Sako, Y.1    Kusumi, A.2
  • 26
    • 12944328730 scopus 로고    scopus 로고
    • Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts
    • Vereb G, et al. (2000) Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts. Proc Natl Acad Sci USA 97:6013-6018.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6013-6018
    • Vereb, G.1
  • 27
    • 0037088647 scopus 로고    scopus 로고
    • Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines
    • Moro L, et al. (2002) Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines. J Biol Chem 277:9405-9414.
    • (2002) J Biol Chem , vol.277 , pp. 9405-9414
    • Moro, L.1
  • 28
    • 0032538798 scopus 로고    scopus 로고
    • Integrins induce activation of EGF receptor: Role in MAP kinase induction and adhesion-dependent cell survival
    • Moro L, et al. (1998) Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion-dependent cell survival. EMBO J 17:6622-6632.
    • (1998) EMBO J , vol.17 , pp. 6622-6632
    • Moro, L.1
  • 29
    • 3042653012 scopus 로고    scopus 로고
    • Integrin regulation of epidermal growth factor (EGF) receptor and of EGF-dependent responses
    • Cabodi S, et al. (2004) Integrin regulation of epidermal growth factor (EGF) receptor and of EGF-dependent responses. Biochem Soc Trans 32:438-442.
    • (2004) Biochem Soc Trans , vol.32 , pp. 438-442
    • Cabodi, S.1
  • 30
    • 17644395663 scopus 로고    scopus 로고
    • The T cell receptor: Critical role of the membrane environment in receptor assembly and function
    • Call ME, Wucherpfennig KW (2005) The T cell receptor: critical role of the membrane environment in receptor assembly and function. Annu Rev Immunol 23:101-125.
    • (2005) Annu Rev Immunol , vol.23 , pp. 101-125
    • Call, M.E.1    Wucherpfennig, K.W.2
  • 31
    • 0023620015 scopus 로고
    • Expression and function of the CD3-antigen receptor on murine CD4+8+ thymocytes
    • Havran WL, et al. (1987) Expression and function of the CD3-antigen receptor on murine CD4+8+ thymocytes. Nature 330:170-173.
    • (1987) Nature , vol.330 , pp. 170-173
    • Havran, W.L.1
  • 32
    • 0023785318 scopus 로고
    • Selective expression of an antigen receptor on CD8-bearing T lymphocytes in transgenic mice
    • Sha WC, et al. (1988) Selective expression of an antigen receptor on CD8-bearing T lymphocytes in transgenic mice. Nature 335:271-274.
    • (1988) Nature , vol.335 , pp. 271-274
    • Sha, W.C.1


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