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Volumn 18, Issue 24, 1999, Pages 6917-6926

Functionally different GPI proteins are organized in different domains on the neuronal surface

Author keywords

Detergent insoluble glycolipid; Neuron; Prion protein; Sphingolipid; Thy 1

Indexed keywords

CELL MEMBRANE PROTEIN; COPPER ION; DETERGENT; GLYCOPROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PHOSPHOLIPID; PRION PROTEIN; SPHINGOLIPID;

EID: 0033573083     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.24.6917     Document Type: Article
Times cited : (334)

References (42)
  • 2
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown, D.A. and London, E. (1998) Structure and origin of ordered lipid domains in biological membranes. J. Membr. Biol., 164, 103-114.
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 3
    • 0026512314 scopus 로고
    • Sorting of GP1-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A. and Rose, J.K. (1992) Sorting of GP1-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
  • 4
    • 0027585161 scopus 로고
    • The molecular biology of the CNTF receptor
    • Davis, S. and Yancopoulos, G.D. (1993) The molecular biology of the CNTF receptor. Curr. Opin. Cell Biol., 5, 281-285.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 281-285
    • Davis, S.1    Yancopoulos, G.D.2
  • 5
    • 0032549668 scopus 로고    scopus 로고
    • T-cadherin is a major glycophosphoinositol-anchored protein associated with noncaveolar detergent-insoluble domains of the cardiac sarcolemma
    • Doyle, D.D., Goings, G.E., Upshaw-Earley, J., Page, E., Ranscht, B. and Palfrey, H.C. (1998) T-cadherin is a major glycophosphoinositol-anchored protein associated with noncaveolar detergent-insoluble domains of the cardiac sarcolemma. J. Biol. Chem., 273, 6937-6943.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6937-6943
    • Doyle, D.D.1    Goings, G.E.2    Upshaw-Earley, J.3    Page, E.4    Ranscht, B.5    Palfrey, H.C.6
  • 6
    • 0030051782 scopus 로고    scopus 로고
    • Thy-1-mediated activation of rat mast cells: The role of Thy-1 membrane microdomains
    • Draberova, L., Amoui, M. and Draber, P. (1996) Thy-1-mediated activation of rat mast cells: the role of Thy-1 membrane microdomains. Immunology, 87, 141-148.
    • (1996) Immunology , vol.87 , pp. 141-148
    • Draberova, L.1    Amoui, M.2    Draber, P.3
  • 7
    • 0028981284 scopus 로고
    • lyn to detergent-resistant membrane domains accompanies cellular signaling
    • lyn to detergent-resistant membrane domains accompanies cellular signaling. Proc. Natl Acad. Sci. USA. 92, 9201-9205.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9201-9205
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 8
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson, T. and Kurzchalia, T.V. (1998) Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature, 394, 802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 9
    • 0029757511 scopus 로고    scopus 로고
    • GP1-anchored proteins, glycosphingolipids and sphingomyelin are sequestered to caveolae only after crosslinking
    • Fujimoto, T. (1996) GP1-anchored proteins, glycosphingolipids and sphingomyelin are sequestered to caveolae only after crosslinking. J. Histochem. Cytochem., 44, 929-941.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 10
    • 0025237057 scopus 로고
    • The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity
    • Furley, A.J., Morton, S.B., Manalo, D., Karagogeos, D., Dodd, J. and Jessell, T.M. (1990) The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity. Cell, 61, 157-170.
    • (1990) Cell , vol.61 , pp. 157-170
    • Furley, A.J.1    Morton, S.B.2    Manalo, D.3    Karagogeos, D.4    Dodd, J.5    Jessell, T.M.6
  • 11
    • 0024361036 scopus 로고
    • Immunoprecipitation of labelled antigens with Eupergit CIZ
    • Grassel, S., Roling, A. and Hasilik, A. (1989) Immunoprecipitation of labelled antigens with Eupergit CIZ. Anal. Biochem., 180, 72-78.
    • (1989) Anal. Biochem. , vol.180 , pp. 72-78
    • Grassel, S.1    Roling, A.2    Hasilik, A.3
  • 12
    • 0019523908 scopus 로고
    • Monoclonal antibody against cell surface glycoprotein of neurons
    • Hirn, M., Pierres, M., Deagostini-Bazin, H., Hirsch, M. and Goridis, C. (1981) Monoclonal antibody against cell surface glycoprotein of neurons. Brain Res., 214, 433-439.
    • (1981) Brain Res. , vol.214 , pp. 433-439
    • Hirn, M.1    Pierres, M.2    Deagostini-Bazin, H.3    Hirsch, M.4    Goridis, C.5
  • 13
    • 0032491910 scopus 로고    scopus 로고
    • Enhanced inhibitory charge transfer during bursts of IPSCs in dentate granule cells in mice with regionally inhibited LTP
    • Hollrigel, G.S., Morris, R.J. and Soltensz, I. (1998) Enhanced inhibitory charge transfer during bursts of IPSCs in dentate granule cells in mice with regionally inhibited LTP. Proc. R. Soc. Lond. B, 265, 63-69.
    • (1998) Proc. R. Soc. Lond. B , vol.265 , pp. 63-69
    • Hollrigel, G.S.1    Morris, R.J.2    Soltensz, I.3
  • 14
    • 12644315046 scopus 로고    scopus 로고
    • -/- mice show augmented TCR signaling and impaired differentiation
    • -/- mice show augmented TCR signaling and impaired differentiation. Curr. Biol., 7, 705-708.
    • (1997) Curr. Biol. , vol.7 , pp. 705-708
    • Hueber, A.O.1
  • 15
    • 0032494242 scopus 로고    scopus 로고
    • Affinity-purification and characterization of caveolins from the brain: Differential expression of caveolin-1, -2 and -3 in brain endothelial and astroglial cell types
    • Ikezu, T. et al. (1998) Affinity-purification and characterization of caveolins from the brain: differential expression of caveolin-1, -2 and -3 in brain endothelial and astroglial cell types. Brain Res., 804, 177-192.
    • (1998) Brain Res. , vol.804 , pp. 177-192
    • Ikezu, T.1
  • 17
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100å using imaging fluorescence resonance energy transfer
    • Kenworthy, A.K. and Edidin, M. (1998) Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100Å 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
  • 19
    • 0344053287 scopus 로고    scopus 로고
    • Oligodendrocytes direct glycosylphosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes
    • Krämer, E.-M., Koch, T., Niehaus, A. and Trotter, J. (1997) Oligodendrocytes direct glycosylphosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes. J. Biol. Chem., 272, 8937-8945.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8937-8945
    • Krämer, E.-M.1    Koch, T.2    Niehaus, A.3    Trotter, J.4
  • 21
    • 0017880184 scopus 로고
    • Molecular weights of the Thy-1 glycoproteins from rat thymus and brain in the presence and absence of deoxycholate
    • Kuchel, P.W., Campbell, D.G., Barclay, A.N. and Willliams, A.F. (1978) Molecular weights of the Thy-1 glycoproteins from rat thymus and brain in the presence and absence of deoxycholate. Biochem. J., 169, 411-417.
    • (1978) Biochem. J. , vol.169 , pp. 411-417
    • Kuchel, P.W.1    Campbell, D.G.2    Barclay, A.N.3    Willliams, A.F.4
  • 22
    • 0017840237 scopus 로고
    • Ganglioside structures and distribution: Are they localized at the nerve ending?
    • Ledeen, R.W. (1978) Ganglioside structures and distribution: are they localized at the nerve ending? J. Supramol. Struct., 8, 1-17.
    • (1978) J. Supramol. Struct. , vol.8 , pp. 1-17
    • Ledeen, R.W.1
  • 23
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor, S., Rothberg, K.G. and Maxfield, F.R. (1994) Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science, 264, 1948-1951.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 24
    • 0029940522 scopus 로고    scopus 로고
    • Cell-surface engineering with GPI-anchored proteins
    • Medof, M.E., Nagarajan, S. and Tykocinski, M.L. (1996) Cell-surface engineering with GPI-anchored proteins. FASEB J., 10, 574-586.
    • (1996) FASEB J. , vol.10 , pp. 574-586
    • Medof, M.E.1    Nagarajan, S.2    Tykocinski, M.L.3
  • 26
    • 0026942291 scopus 로고
    • Thy-1, the enigmatic extrovert on the neuronal surface
    • Morris, R. (1992) Thy-1, the enigmatic extrovert on the neuronal surface. BioEssays, 14, 715-722.
    • (1992) BioEssays , vol.14 , pp. 715-722
    • Morris, R.1
  • 27
    • 0020544784 scopus 로고
    • Fixation of Thy-1 in nervous tissue for immunohistochemistry: A quantitative assessment of the effect of different fixation conditions upon retention of antigenicity and the cross-linking of Thy-1
    • Morris, R.J. and Barber, P.C. (1983) Fixation of Thy-1 in nervous tissue for immunohistochemistry: a quantitative assessment of the effect of different fixation conditions upon retention of antigenicity and the cross-linking of Thy-1. J. Histochem. Cytochem., 31, 263-274.
    • (1983) J. Histochem. Cytochem. , vol.31 , pp. 263-274
    • Morris, R.J.1    Barber, P.C.2
  • 28
    • 0028902465 scopus 로고
    • Developmental expression of the prion protein gene in glial cells
    • Moser, M., Colello, R.J., Pott, U. and Oesch, B. (1995) Developmental expression of the prion protein gene in glial cells. Neuron, 14, 509-517.
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moser, M.1    Colello, R.J.2    Pott, U.3    Oesch, B.4
  • 29
    • 13344282736 scopus 로고    scopus 로고
    • Normal spatial learning despite regional inhibition of LTP in mice lacking Thy-1
    • Nosten-Bertrand, M. et al. (1996) Normal spatial learning despite regional inhibition of LTP in mice lacking Thy-1. Nature, 379, 826-829.
    • (1996) Nature , vol.379 , pp. 826-829
    • Nosten-Bertrand, M.1
  • 30
    • 0001353920 scopus 로고
    • Purified α2-macroglobulin receptor/LDL receptor related protein binds urokinase plasminogen activator inhibitor type-1 complex: Evidence that the α2-macroglobulin receptor mediates cellular degradation of urokinase receptor-bound complexes
    • Nykjaer, A. et al. (1992) Purified α2-macroglobulin receptor/LDL receptor related protein binds urokinase plasminogen activator inhibitor type-1 complex: evidence that the α2-macroglobulin receptor mediates cellular degradation of urokinase receptor-bound complexes. J. Biol. Chem., 267, 14543-14546.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14543-14546
    • Nykjaer, A.1
  • 31
    • 0028805468 scopus 로고
    • The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum
    • Olive, S., Dubois, C., Schachner, M. and Rougon, G. (1995) The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum. J. Neurochem., 65, 2307-2317.
    • (1995) J. Neurochem. , vol.65 , pp. 2307-2317
    • Olive, S.1    Dubois, C.2    Schachner, M.3    Rougon, G.4
  • 32
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P.C. and Harris, D.A. (1998) Copper stimulates endocytosis of the prion protein. J. Biol. Chem., 273, 33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 34
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • Rietveld, A. and Simons, K. (1998) The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim. Biophys. Acta, 1376, 467-479.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 467-479
    • Rietveld, A.1    Simons, K.2
  • 36
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer, J.E., McIntosh, D.P., Dvorak, A.M., Liu, J. and Oh, P. (1995) Separation of caveolae from associated microdomains of GPI-anchored proteins. Science, 269, 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
  • 37
    • 0030606019 scopus 로고    scopus 로고
    • The localization of gangliosides in neurons of the central nervous system: The use of anti-ganglioside antibodies
    • Schwarz, A. and Futerman, A.H. (1996) The localization of gangliosides in neurons of the central nervous system: the use of anti-ganglioside antibodies. Biochim. Biophys. Acta, 1286, 247-267.
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 247-267
    • Schwarz, A.1    Futerman, A.H.2
  • 38
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets, E.D., Lee, G.M., Simson, R. and 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
  • 41
    • 0028360654 scopus 로고
    • The mode of anchorage to the cell surface determines both the function and membrane location of Thy-1 glycoprotein
    • Tiveron, M.C., Nosten-Bertrand, M., Jani, H., Garnett, D., Hirst, E.M.A., Grosveld, F. and Morris, R.J. (1994) The mode of anchorage to the cell surface determines both the function and membrane location of Thy-1 glycoprotein. J. Cell Sci., 107, 1783-1796.
    • (1994) J. Cell Sci. , vol.107 , pp. 1783-1796
    • Tiveron, M.C.1    Nosten-Bertrand, M.2    Jani, H.3    Garnett, D.4    Hirst, E.M.A.5    Grosveld, F.6    Morris, R.J.7
  • 42
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R. and 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


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