메뉴 건너뛰기




Volumn 21, Issue 3, 2004, Pages 193-205

Plasma membrane microdomains: Organization, function and trafficking (Review)

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; CLATHRIN; LIPID;

EID: 2942625797     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/09687680410001700517     Document Type: Review
Times cited : (175)

References (143)
  • 1
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid-cholesterol rich detergent-insoluble domains in cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes
    • Ahmed, S. N., Brown, D. A. and London, E., 1997, On the origin of sphingolipid-cholesterol rich detergent-insoluble domains in cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes. Biochemistry, 36, 10944-10953.
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 2
    • 0037458140 scopus 로고    scopus 로고
    • Regulation of integrin growth factor interactions in oligodendrocytes by lipid raft microdomains
    • Baron, W., Decker, L., Colognato, H. and ffrench-Constant, C., 2003, Regulation of integrin growth factor interactions in oligodendrocytes by lipid raft microdomains. Curr. Biol., 13, 151-155.
    • (2003) Curr. Biol. , vol.13 , pp. 151-155
    • Baron, W.1    Decker, L.2    Colognato, H.3    Ffrench-Constant, C.4
  • 3
    • 0030982565 scopus 로고    scopus 로고
    • Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol
    • Bist, A., Fielding, P. E. and Fielding, C. J., 1997, Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol. Proc. Natl Acad. Sci. USA, 94, 10693-10698.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10693-10698
    • Bist, A.1    Fielding, P.E.2    Fielding, C.J.3
  • 4
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A. and 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
  • 5
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipids-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. A. and Rose, J. K., 1992, Sorting of GPI-anchored proteins to glycolipids-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
  • 6
    • 0034529950 scopus 로고    scopus 로고
    • In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
    • Bucci, M., Gratton, J. P., Rudic, R. D., Acevedo, L., Roviezzo, F., Cirino, G. and Sessa, W. C., 2000, In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation. Nat. Med., 6, 1362-1367.
    • (2000) Nat. Med. , vol.6 , pp. 1362-1367
    • Bucci, M.1    Gratton, J.P.2    Rudic, R.D.3    Acevedo, L.4    Roviezzo, F.5    Cirino, G.6    Sessa, W.C.7
  • 9
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported bilayer model membranes
    • Dietrich, C., Volovyk, Z. N., Levi, M., Thompson, N. L. and Jacobson, K., 2001b, Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported bilayer model membranes. Proc. Natl Acad. Sci. USA, 98, 10642-10647.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10642-10647
    • Dietrich, C.1    Volovyk, Z.N.2    Levi, M.3    Thompson, N.L.4    Jacobson, K.5
  • 10
    • 0036214457 scopus 로고    scopus 로고
    • Relationship of lipid rafts to transient confinement zones detected by single particle tracking
    • Dietrich, C., Yang, B., Fujiwara, T., Kusumi, A. and Jacobson, K., 2002, Relationship of lipid rafts to transient confinement zones detected by single particle tracking. Biophys. J., 82, 274-284.
    • (2002) Biophys. J. , vol.82 , pp. 274-284
    • Dietrich, C.1    Yang, B.2    Fujiwara, T.3    Kusumi, A.4    Jacobson, K.5
  • 12
    • 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
  • 13
    • 0028325756 scopus 로고
    • Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins
    • Edidin, M., Zuniga, M. C. and Sheetz, M. P., 1994, Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins. Proc. Natl Acad. Sci. USA, 91, 3378-3382.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3378-3382
    • Edidin, M.1    Zuniga, M.C.2    Sheetz, M.P.3
  • 14
    • 0028981284 scopus 로고
    • Fc epsilon RI-medieated recruitment of p53/56lyn to detergent resistant membrane domains accompanies cellualar signalling
    • Field, K. A., Holowka, D. and Baird, B., 1995, Fc epsilon RI-medieated recruitment of p53/56lyn to detergent resistant membrane domains accompanies cellualar signalling. 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
  • 15
    • 0033596725 scopus 로고    scopus 로고
    • Intracellular cholesterol transport in synchronized human skin fibroblasts
    • Fielding, C. J., Bist, A. and Fielding, P. E., 1999, Intracellular cholesterol transport in synchronized human skin fibroblasts. Biochemistry, 38, 2506-2513.
    • (1999) Biochemistry , vol.38 , pp. 2506-2513
    • Fielding, C.J.1    Bist, A.2    Fielding, P.E.3
  • 16
    • 0037216768 scopus 로고    scopus 로고
    • Molecular mechanisms involved in the regulation of the endothelial nitric oxide synthase
    • Fleming, I. and Busse, R., 2003, Molecular mechanisms involved in the regulation of the endothelial nitric oxide synthase. Am. J. Physiol. Regul. Integr. Comp. Physiol., 284, R1-R12.
    • (2003) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.284
    • Fleming, I.1    Busse, R.2
  • 17
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L. J., De Hoog, C. L. and Mann, M., 2003, Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl Acad. Sci. USA, 100, 5813-5818.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 18
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin
    • Fra, A. M., Williamson, E., Simons, K. and Parton, R. G., 1995, De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc. Natl Acad. Sci. USA, 92, 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
  • 19
    • 0033975048 scopus 로고    scopus 로고
    • Genomic organization and transcriptional analysis of the human genes coding for caveolin-1 and caveolin-2
    • Fra, A. M., Pasqualetto, E., Mancini, M. and Sitia, R., 2000, Genomic organization and transcriptional analysis of the human genes coding for caveolin-1 and caveolin-2. Gene, 243, 75-83.
    • (2000) Gene , vol.243 , pp. 75-83
    • Fra, A.M.1    Pasqualetto, E.2    Mancini, M.3    Sitia, R.4
  • 20
    • 0033594934 scopus 로고    scopus 로고
    • Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem high-resolution mass spectrometry
    • Fridriksson, E. K., Shipkova, P. A., Sheets, E. D., Holowka, D., Baird, B. and McLafferty, F. W., 1999, Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem high-resolution mass spectrometry. Biochemistry, 38, 8056-8063.
    • (1999) Biochemistry , vol.38 , pp. 8056-8063
    • Fridriksson, E.K.1    Shipkova, P.A.2    Sheets, E.D.3    Holowka, D.4    Baird, B.5    McLafferty, F.W.6
  • 21
    • 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
  • 22
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara, T., Ritchie, K., Murakoshi, H., Jacobson, K. and Kusumi, A., 2002, Phospholipids undergo hop diffusion in compartmentalized cell membrane. J. Cell Biol., 157, 1071-1081.
    • (2002) J. Cell Biol. , vol.157 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 23
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase
    • Furuchi, T. and Anderson, R. G. W., 1998, Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase. J. Biol. Chem., 274, 30636-30643.
    • (1998) J. Biol. Chem. , vol.274 , pp. 30636-30643
    • Furuchi, T.1    Anderson, R.G.W.2
  • 24
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44MAP kinase cascade
    • Galbiati, F., 1998, Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44MAP kinase cascade. EMBO J., 17, 6633-6648.
    • (1998) EMBO J. , vol.17 , pp. 6633-6648
    • Galbiati, F.1
  • 25
    • 0035877753 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities
    • Galbiati, F., Engelman, J. A., Volonte, D., Zhang, X. L., Minetti, C., Li, M., Hou, H., Kneitz, B., Edelmann, W. and Lisanti, M. P., 2001, Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities. J. Biol. Chem., 276, 21425-21433.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21425-21433
    • Galbiati, F.1    Engelman, J.A.2    Volonte, D.3    Zhang, X.L.4    Minetti, C.5    Li, M.6    Hou, H.7    Kneitz, B.8    Edelmann, W.9    Lisanti, M.P.10
  • 26
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the non caveolin binding domain in vivo
    • Garcia-Cardena, G., Martasek, P., Masters, B. S., Skidd, P. M., Couet, J., Li, S., Lisanti, M. P. and Sessa, W. C., 1997, Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the non caveolin binding domain in vivo. J. Biol. Chem., 272, 25437-25440.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25437-25440
    • Garcia-Cardena, G.1    Martasek, P.2    Masters, B.S.3    Skidd, P.M.4    Couet, J.5    Li, S.6    Lisanti, M.P.7    Sessa, W.C.8
  • 28
    • 0035929567 scopus 로고    scopus 로고
    • The T cell receptor for antigen: Signaling and ligand discrimination
    • Germain, R. N., 2001, The T cell receptor for antigen: signaling and ligand discrimination. J. Biol. Chem., 276, 35223-35226.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35223-35226
    • Germain, R.N.1
  • 30
    • 0034675889 scopus 로고    scopus 로고
    • Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies
    • Harder, T. and Kuhn, M., 2000, Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies. J. Cell Biol., 151, 199-208.
    • (2000) J. Cell Biol. , vol.151 , pp. 199-208
    • Harder, T.1    Kuhn, M.2
  • 31
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domains formation in lipid raft mixtures
    • Heerklotz, H., 2002, Triton promotes domains formation in lipid raft mixtures. Biophys. J., 83, 2693-2701.
    • (2002) Biophys. J. , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 32
    • 0015714290 scopus 로고
    • Comparison of the tissue receptors for Vibrio cholerae and Escherichia coli enterotoxins by means of gangliosides and natural cholera toxoid
    • Holmgren, J., 1973, Comparison of the tissue receptors for Vibrio cholerae and Escherichia coli enterotoxins by means of gangliosides and natural cholera toxoid. Infect. Immun., 8, 851-859.
    • (1973) Infect. Immun. , vol.8 , pp. 851-859
    • Holmgren, J.1
  • 35
    • 0014312862 scopus 로고
    • Formation of elaborate networks of T-system tubules in cultured skeletal muscle with special reference to the T-system formation
    • Ishikawa, H., 1968, Formation of elaborate networks of T-system tubules in cultured skeletal muscle with special reference to the T-system formation. J. Cell Biol., 38, 51-66.
    • (1968) J. Cell Biol. , vol.38 , pp. 51-66
    • Ishikawa, H.1
  • 36
    • 0033429208 scopus 로고    scopus 로고
    • Calcium signal transduction from caveolae
    • Isshiki, M. and Anderson, R. G., 1999, Calcium signal transduction from caveolae. Cell Calcium, 26, 201-208.
    • (1999) Cell Calcium , vol.26 , pp. 201-208
    • Isshiki, M.1    Anderson, R.G.2
  • 37
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes, P. W., Ley, S. C. and Magee, A. I., 1999, Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J. Cell Biol., 147, 447-461.
    • (1999) J. Cell Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 38
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • Kabouridis, P. S., Magee, A. I. and Ley, S. C., 1997, S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO J., 16, 4983-4998.
    • (1997) EMBO J. , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 39
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycophosphatidylinositol-anchored protein at the apical surface of MDCK cell examined at a reolution of < 100Å using imaging fluorescence resonance energy transfer
    • Kenworthy, A. K. and Edidin, M., 1998, Distribution of a glycophosphatidylinositol-anchored protein at the apical surface of MDCK cell examined at a reolution 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
  • 40
    • 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
  • 41
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia, T. V., Dupree, P., Parton, R. G., Kellner, R., Virta, H., Lehnert, M. and Simons, K., 1992, VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J. Cell Biol., 118, 1003-1014.
    • (1992) J. Cell Biol. , vol.118 , pp. 1003-1014
    • Kurzchalia, T.V.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 42
    • 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. and 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
  • 43
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin
    • Kwik, J., Boyle, S., Fooksman, D., Margolis, L., Sheetz, M. P. and Edidin, M., 2003, Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin. Proc. Natl Acad. Sci. USA, 100, 13964-13969.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Edidin, M.6
  • 44
    • 0037434839 scopus 로고    scopus 로고
    • Involvement of caveolin-2 in caveolar biogenesis in MDCK cells
    • Lahtinen, U., Honsho, M., Parton, R. G., Simons, K. and Verkade, P., 2003, Involvement of caveolin-2 in caveolar biogenesis in MDCK cells. FEBS Lett., 538, 85-88.
    • (2003) FEBS Lett. , vol.538 , pp. 85-88
    • Lahtinen, U.1    Honsho, M.2    Parton, R.G.3    Simons, K.4    Verkade, P.5
  • 45
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • Lang, T., Bruns, D., Wenzel, D., Riedel, D., Holroyd, P., Thiele, C. and Jahn, R., 2001, SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J., 20, 2202-2213.
    • (2001) EMBO J. , vol.20 , pp. 2202-2213
    • Lang, T.1    Bruns, D.2    Wenzel, D.3    Riedel, D.4    Holroyd, P.5    Thiele, C.6    Jahn, R.7
  • 46
    • 0036479204 scopus 로고    scopus 로고
    • Caveolin-1 is a negative regulator of caveolae-mediated endocytosis to the endoplasmic reticulum
    • Le, P. U., Guay, G., Altschuler, Y. and Nabi, I. R., 2002, Caveolin-1 is a negative regulator of caveolae-mediated endocytosis to the endoplasmic reticulum. J. Biol. Chem., 277, 3371-3379.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3371-3379
    • Le, P.U.1    Guay, G.2    Altschuler, Y.3    Nabi, I.R.4
  • 47
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • Lisanti, M. P., Scherer, P. E., Tang, Z. L. and Sargiacomo, M., 1994, Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis. Trends Cell Biol., 4, 231-235.
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.L.3    Sargiacomo, M.4
  • 48
    • 0029879507 scopus 로고    scopus 로고
    • Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae
    • Liu, P., Ying, Y., Ko, Y. G. and Anderson, R. G., 1996, Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae. J. Biol. Chem., 271, 10299-10303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10299-10303
    • Liu, P.1    Ying, Y.2    Ko, Y.G.3    Anderson, R.G.4
  • 49
    • 0036667737 scopus 로고    scopus 로고
    • Insights into lipid raft structure and formation from experiments in model membranes
    • London, E., 2002, Insights into lipid raft structure and formation from experiments in model membranes. Curr. Opin. Struct. Biol., 12, 480-486.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 480-486
    • London, E.1
  • 50
    • 0035200238 scopus 로고    scopus 로고
    • N-terminal protein acylation confers localization to cholesterol, sphingolipid-enriched membranes but not to lipid rafts/caveolae
    • McCabe, J. B. and Berthiaume, L. G., 2001, N-terminal protein acylation confers localization to cholesterol, sphingolipid-enriched membranes but not to lipid rafts/caveolae. Mol. Biol. Cell, 12, 3601-3617.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3601-3617
    • McCabe, J.B.1    Berthiaume, L.G.2
  • 51
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore, N., Smith, K. L., Graham, C. H., Jen, A., Brady, K., Hall, S. and Morris, R., 1999, Functionally different GPI proteins are organized in different domains on the neuronal surface. EMBO J., 18, 6917-6926.
    • (1999) EMBO J. , vol.18 , pp. 6917-6926
    • Madore, N.1    Smith, K.L.2    Graham, C.H.3    Jen, A.4    Brady, K.5    Hall, S.6    Morris, R.7
  • 52
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many 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 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
  • 53
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffet, S., Brown, D. A. and Linder, M. E., 2000, Lipid-dependent targeting of G proteins into rafts. J. Biol. Chem., 275, 2191-2198.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2191-2198
    • Moffet, S.1    Brown, D.A.2    Linder, M.E.3
  • 54
    • 0028998554 scopus 로고
    • VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro
    • Monier, S., Parton, R. G., Vogel, F., Behlke, J., Henske, A. and Kurzchalia, T. V., 1995, VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro. Mol. Biol. Cell, 6, 911-927.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 911-927
    • Monier, S.1    Parton, R.G.2    Vogel, F.3    Behlke, J.4    Henske, A.5    Kurzchalia, T.V.6
  • 55
    • 0019994630 scopus 로고
    • Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins
    • Montesano, R., Roth, J., Robert, A. and Orci, L., 1982, Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins. Nature, 296, 651-653.
    • (1982) Nature , vol.296 , pp. 651-653
    • Montesano, R.1    Roth, J.2    Robert, A.3    Orci, L.4
  • 56
    • 0032530369 scopus 로고    scopus 로고
    • Engagement of T-cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains
    • Montixi, C., 1998, Engagement of T-cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains. EMBO J., 17, 5334-5348.
    • (1998) EMBO J. , vol.17 , pp. 5334-5348
    • Montixi, C.1
  • 57
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro, S., 2003, Lipid rafts: elusive or illusive? Cell, 115, 377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 59
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray, D., Ben-Tal, N., Honig, B. and McLaughlin, S., 1997, Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure, 5, 985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 60
    • 0032763121 scopus 로고    scopus 로고
    • Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: Theory and experiment
    • Murray, D., Arbuzova, A., Hangyas-Mihalyne, G., Gambhir, A., Ben-Tal, N., Honig, B. and McLaughlin, S., 1999, Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: theory and experiment. Biophys. J., 77, 3176-3188.
    • (1999) Biophys. J. , vol.77 , pp. 3176-3188
    • Murray, D.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    Gambhir, A.4    Ben-Tal, N.5    Honig, B.6    McLaughlin, S.7
  • 61
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • Nabi, I. R. and Le, P. U., 2003, Caveolae/raft-dependent endocytosis. J. Cell Biol., 161, 673-677.
    • (2003) J. Cell Biol. , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 62
    • 0036094927 scopus 로고    scopus 로고
    • A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex
    • Nichols, B. J., 2002, A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex. Nat. Cell Biol., 4, 374-378.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 374-378
    • Nichols, B.J.1
  • 63
    • 0345706824 scopus 로고    scopus 로고
    • Caveosomes and endocytosis of lipid rafts
    • Nichols, B. J., 2003, Caveosomes and endocytosis of lipid rafts. J. Cell Sci., 116, 4707-4714.
    • (2003) J. Cell Sci. , vol.116 , pp. 4707-4714
    • Nichols, B.J.1
  • 65
    • 0037182579 scopus 로고    scopus 로고
    • Activated K-ras and H-ras display different interactions with saturable nonraft sites at the surface of live cells
    • Niv, H., Gutman, O., Kloog, Y. and Henis, Y., 2002, Activated K-ras and H-ras display different interactions with saturable nonraft sites at the surface of live cells. J. Cell Biol., 157, 865-872.
    • (2002) J. Cell Biol. , vol.157 , pp. 865-872
    • Niv, H.1    Gutman, O.2    Kloog, Y.3    Henis, Y.4
  • 66
    • 0031590153 scopus 로고    scopus 로고
    • Two-dimensional distribution of Gi2a in the plasma membrane: A critical evaluation by immunocytochemistry
    • Nomura, R., Inuo, C., Takahashi, Y., Asano, T. and Fujimoto, T., 1997, Two-dimensional distribution of Gi2a in the plasma membrane: a critical evaluation by immunocytochemistry. FEBS Lett., 415, 139-144.
    • (1997) FEBS Lett. , vol.415 , pp. 139-144
    • Nomura, R.1    Inuo, C.2    Takahashi, Y.3    Asano, T.4    Fujimoto, T.5
  • 67
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh, P., McInitosh, D. P. and Schnitzer, J. E., 1998, Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol., 141, 101-114.
    • (1998) J. Cell Biol. , vol.141 , pp. 101-114
    • Oh, P.1    McInitosh, D.P.2    Schnitzer, J.E.3
  • 68
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing 'pre-assembled signaling complexes' at the plasma membrane
    • Okamoto, T., Schlegel, A., Scherer, P. E. and Lisanti, M. P., 1998, Caveolins, a family of scaffolding proteins for organizing 'pre-assembled signaling complexes' at the plasma membrane. J. Biol. Chem., 273, 5419-5422.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 69
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: Evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi, P. A. and Fishman, P. H., 1998, Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J. Cell Biol., 141, 905-915.
    • (1998) J. Cell Biol. , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 70
    • 0000855817 scopus 로고
    • Fine structure of blood capillaries
    • Palade, G. E., 1953, Fine structure of blood capillaries. J. Appl. Phys., 24, 1424.
    • (1953) J. Appl. Phys. , vol.24 , pp. 1424
    • Palade, G.E.1
  • 72
    • 0030222108 scopus 로고    scopus 로고
    • Caveolae and caveolins
    • Parton, R. G., 1996, Caveolae and caveolins. Curr. Opin. Cell Biol., 8, 542-548.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 542-548
    • Parton, R.G.1
  • 73
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • Parton, R. G. and Richards, A. A., 2003, Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic, 4, 724-738.
    • (2003) Traffic , vol.4 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 74
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton, R. G., Joggerst, B. and Simons, K., 1994, Regulated internalization of caveolae. J. Cell Biol., 127, 1199-1215.
    • (1994) J. Cell Biol. , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 75
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans, L., Kartenbeck, J. and Helenius, A., 2001, Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol., 3, 473-483.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 76
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans, L., Puntener, D. and Helenius, A., 2002, Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science, 296, 535-539.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 77
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains
    • Pike, L. J. and Casey, L., 1996, Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains. J. Biol. Chem., 271, 26453-26456.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26453-26456
    • Pike, L.J.1    Casey, L.2
  • 78
    • 0032575524 scopus 로고    scopus 로고
    • Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover
    • Pike, L. J. and Miller, J. M., 1998, Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover. J. Biol. Chem., 273, 22298-22304.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22298-22304
    • Pike, L.J.1    Miller, J.M.2
  • 79
    • 0037065727 scopus 로고    scopus 로고
    • Lipid rafts are enriched in arachidonic acid and plasmenylethanolamine and their composition is independent of caveolin-1 expression: A quantitative electrospray ionization/mass spectrometric analysis
    • Pike, L. J., Han, X., Chung, K. N. and Gross, R. W., 2002, Lipid rafts are enriched in arachidonic acid and plasmenylethanolamine and their composition is independent of caveolin-1 expression: a quantitative electrospray ionization/mass spectrometric analysis. Biochemistry, 41, 2075-2088.
    • (2002) Biochemistry , vol.41 , pp. 2075-2088
    • Pike, L.J.1    Han, X.2    Chung, K.N.3    Gross, R.W.4
  • 80
    • 0035809933 scopus 로고    scopus 로고
    • A caveolin dominant-negative mutant associates with lipid bodies on the caveolin-cycling pathway and induces intracellular cholesterol imbalance
    • Pol, A., Luetterforst, R., Lindsay, M. R., Heino, S., Ikonen, E. and Parton, R. G., 2001, A caveolin dominant-negative mutant associates with lipid bodies on the caveolin-cycling pathway and induces intracellular cholesterol imbalance. J. Cell Biol., 152, 1057-1070.
    • (2001) J. Cell Biol. , vol.152 , pp. 1057-1070
    • Pol, A.1    Luetterforst, R.2    Lindsay, M.R.3    Heino, S.4    Ikonen, E.5    Parton, R.G.6
  • 81
    • 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
  • 82
    • 0035067187 scopus 로고    scopus 로고
    • GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
    • Prior, I. A., Harding, A., Yan, J., Sluimer, J., Parton, R. G. and Hancock, J. F., 2001, GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat. Cell Biol., 3, 368-375.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 368-375
    • Prior, I.A.1    Harding, A.2    Yan, J.3    Sluimer, J.4    Parton, R.G.5    Hancock, J.F.6
  • 83
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior, I. A., Muncke, C., Parton, R. G. and Hancock, J. F., 2003, Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol., 160, 165-170.
    • (2003) J. Cell Biol. , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 87
    • 0033597141 scopus 로고    scopus 로고
    • Association of sterol- and glycophosphatidylinositol-linked proteins with Drosophila raft microdomains
    • Rietveld, A., Neutz, S., Simons, K. and Eaton, S., 1999, Association of sterol- and glycophosphatidylinositol-linked proteins with Drosophila raft microdomains. J. Biol. Chem., 274, 12049-12054.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12049-12054
    • Rietveld, A.1    Neutz, S.2    Simons, K.3    Eaton, S.4
  • 88
    • 0037087555 scopus 로고    scopus 로고
    • Cholesterol is important in control of EGF-receptor kinase activity but EGF receptors are not concentrated in caveolae
    • Ringerike, T., Blystad, F. D., Levy, F. O., Madshus, I. H. and Stang, E., 2002, Cholesterol is important in control of EGF-receptor kinase activity but EGF receptors are not concentrated in caveolae. J. Cell Sci., 115, 1331-1340.
    • (2002) J. Cell Sci. , vol.115 , pp. 1331-1340
    • Ringerike, T.1    Blystad, F.D.2    Levy, F.O.3    Madshus, I.H.4    Stang, E.5
  • 89
    • 0346997045 scopus 로고    scopus 로고
    • The fence and picket structure of the plasma membrane of live cells as revealed by single molecule techniques
    • Ritchie, K., Iino, R., Fujiwara, T., Murase, K. and Kusumi, A., 2003, The fence and picket structure of the plasma membrane of live cells as revealed by single molecule techniques. Mol. Membr. Biol., 20, 13-18.
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 13-18
    • Ritchie, K.1    Iino, R.2    Fujiwara, T.3    Murase, K.4    Kusumi, A.5
  • 90
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-b-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles
    • Rodal, S. K., Skretting, G., Garred, Ø., Vilhardt, F., van Deurs, B. and Sandvig, K., 1999, Extraction of cholesterol with methyl-b-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles. Mol. Biol. Cell, 10, 961-974.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Garred, Ø.3    Vilhardt, F.4    Van Deurs, B.5    Sandvig, K.6
  • 91
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • Rothberg, K. G., Ying, Y. S., Kamen, B. A. and Anderson, R. G., 1990, Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate. J. Cell Biol., 111, 2931-2938.
    • (1990) J. Cell Biol. , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.S.2    Kamen, B.A.3    Anderson, R.G.4
  • 94
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated clathrin-idependent pinocytic pathway
    • Sabharanjak, S., Sharma, P., Parton, R. G. and Mayor, S., 2002, GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated clathrin-idependent pinocytic pathway. Dev. Cell, 2, 411-423.
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 95
    • 0028243194 scopus 로고
    • Compartmentalized structure of the plasma-membrane for receptor movements as revealed by a nanometer-level motion analysis
    • Sako, Y. and 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
  • 96
    • 0034859215 scopus 로고    scopus 로고
    • Characterization of cholesterol-sphingomyelin domains and their dynamics in bilayer membranes
    • Samsonov, A. V., Mihalyov, I. and Cohen, F. S., 2001, Characterization of cholesterol-sphingomyelin domains and their dynamics in bilayer membranes. Biophys. J., 81, 1486-1500.
    • (2001) Biophys. J. , vol.81 , pp. 1486-1500
    • Samsonov, A.V.1    Mihalyov, I.2    Cohen, F.S.3
  • 97
    • 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. and Lisanti, M. P., 1993, Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol., 122, 789-807.
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 98
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistence on lipids and GPI-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behaviour
    • Schroeder, R., London, E. and Brown, D. A., 1994, Interactions between saturated acyl chains confer detergent resistence on lipids and GPI-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behaviour. Proc. Natl Acad. Sci. USA, 91, 12130-12134.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.A.3
  • 99
    • 0035965995 scopus 로고    scopus 로고
    • Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo
    • Schubert, W., Frank, P. G., Razani, B., Park, D. S., Chow, C. W. and Lisanti, M. P., 2001, Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo. J. Biol. Chem., 276, 48619-48622.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48619-48622
    • Schubert, W.1    Frank, P.G.2    Razani, B.3    Park, D.S.4    Chow, C.W.5    Lisanti, M.P.6
  • 101
    • 0037874731 scopus 로고    scopus 로고
    • Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • Schutz, G. J., Kada, G., Pastushenko, V. P. and 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
    • Schutz, G.J.1    Kada, G.2    Pastushenko, V.P.3    Schindler, H.4
  • 102
    • 0037470170 scopus 로고    scopus 로고
    • Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling
    • Sharma, D. K., Choudhary, A., Singh, R. D., Wheatley, C. L., Marks, D. L. and Pagano, R. E., 2003, Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling. J. Biol. Chem., 278, 7564-7572.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7564-7572
    • Sharma, D.K.1    Choudhary, A.2    Singh, R.D.3    Wheatley, C.L.4    Marks, D.L.5    Pagano, R.E.6
  • 103
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma, P., Varma, R., Sarasij, R. C., Ira, Gousset, K., Krishnamoorthy, G., Rao, M. and Mayor, S., 2004, Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell, 116, 577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira4    Gousset, K.5    Krishnamoorthy, G.6    Rao, M.7    Mayor, S.8
  • 105
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets, E. D., Lee, G. M., Simson, K. 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, K.3    Jacobson, K.4
  • 106
    • 0033577805 scopus 로고    scopus 로고
    • Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FceRI and their association with detergent-resistant membranes
    • Sheets, E. D., Holowka, D. and Baird, B., 1999, Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FceRI and their association with detergent-resistant membranes. J. Cell Biol., 145, 877-887.
    • (1999) J. Cell Biol. , vol.145 , pp. 877-887
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 107
    • 0141828502 scopus 로고    scopus 로고
    • Use of detergent to study membrane rafts: The good, the bad, and the ugly
    • Shogomori, H. and Brown, D. A., 2003, Use of detergent to study membrane rafts: the good, the bad, and the ugly. Biol. Chem., 384, 1259-1263.
    • (2003) Biol. Chem. , vol.384 , pp. 1259-1263
    • Shogomori, H.1    Brown, D.A.2
  • 108
    • 0037429735 scopus 로고    scopus 로고
    • Role of cholesterol in lipid raft formation: Lessons from lipid model systems
    • Silvius, J. R., 2003, Role of cholesterol in lipid raft formation: lessons from lipid model systems. Biochim. Biophys. Acta, 1610, 174-183.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 174-183
    • Silvius, J.R.1
  • 109
    • 0029906007 scopus 로고    scopus 로고
    • Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length
    • Silvius, J. R., del Giudice, D. and Lafleur, M., 1996, Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length. Biochemistry, 35, 15198-15208.
    • (1996) Biochemistry , vol.35 , pp. 15198-15208
    • Silvius, J.R.1    Del Giudice, D.2    Lafleur, M.3
  • 110
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K. and 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
  • 111
  • 112
    • 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
  • 113
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K. and Wandinger-Ness, A., 1990, Polarized sorting in epithelia. Cell, 62, 207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 114
    • 0029162080 scopus 로고
    • Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis
    • Simson, R., Sheets, E. D. and 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.D.2    Jacobson, K.3
  • 116
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S. J. and Nicholson, G. L., 1972, The fluid mosaic model of the structure of cell membranes. Science, 175, 720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicholson, G.L.2
  • 117
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart, E. J., Ying, Y., Donzell, W. C. and Anderson, R. G. W., 1996, A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J. Biol. Chem., 271, 29427-29435.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29427-29435
    • Smart, E.J.1    Ying, Y.2    Donzell, W.C.3    Anderson, R.G.W.4
  • 118
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
    • Song, S. K., Li, S., Okamoto, T., Quilliam, L. A., Sargiacomo, M. and Lisanti, M. P., 1996, Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains. J. Biol. Chem., 271, 9690-9697.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, S.K.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 119
    • 0039493929 scopus 로고    scopus 로고
    • Targeting of a G alpha subunit (Gi1 alpha) and c-Src tyrosine kinase to caveolae membranes: Clarifying the role of N-myristoylation
    • Song, K. S., Sargiacomo, M., Galbiati, F., Parenti, M. and Lisanti, M. P., 1997, Targeting of a G alpha subunit (Gi1 alpha) and c-Src tyrosine kinase to caveolae membranes: clarifying the role of N-myristoylation. Cell Mol. Biol. (Noisy-le-grand), 43, 293-303.
    • (1997) Cell Mol. Biol. (Noisy-le-grand) , vol.43 , pp. 293-303
    • Song, K.S.1    Sargiacomo, M.2    Galbiati, F.3    Parenti, M.4    Lisanti, M.P.5
  • 121
    • 0038313015 scopus 로고    scopus 로고
    • The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation
    • Sowa, G., Pypaert, M., Fulton, D. and Sessa, W. C., 2003, The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation. Proc. Natl Acad. Sci. USA, 100, 6511-6516.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6511-6516
    • Sowa, G.1    Pypaert, M.2    Fulton, D.3    Sessa, W.C.4
  • 122
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer, T. P. and Meyer, T., 1997, Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol., 139, 1447-1454.
    • (1997) J. Cell Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 123
    • 0037429658 scopus 로고    scopus 로고
    • Dynamics of raft molecules in the cell and artificial membranes: Approaches by pulse EPR spin labeling and single molecule optical microscopy
    • Subczynski, W. K. and Kusumi, A., 2003, Dynamics of raft molecules in the cell and artificial membranes: approaches by pulse EPR spin labeling and single molecule optical microscopy. Biochim. Biophys. Acta, 1610, 231-243.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 231-243
    • Subczynski, W.K.1    Kusumi, A.2
  • 125
    • 0028352175 scopus 로고
    • Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins
    • Thomas, J. L., Holowka, D., Baird, B. and Webb, W. W., 1994, Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins. J. Cell Biol., 125, 795-802.
    • (1994) J. Cell Biol. , vol.125 , pp. 795-802
    • Thomas, J.L.1    Holowka, D.2    Baird, B.3    Webb, W.W.4
  • 126
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains which are not involved in constitutive endocytic trafficking
    • Thomsen, P., Roepstorff, K., Stahlhut, M. and van Deurs, B., 2002, Caveolae are highly immobile plasma membrane microdomains which are not involved in constitutive endocytic trafficking. Mol. Biol. Cell, 13, 238-250.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    Van Deurs, B.4
  • 127
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen, M. L., Skretting, G., van Deurs, B. and Sandvig, K., 2001, Internalization of cholera toxin by different endocytic mechanisms. J. Cell Sci., 114, 3737-3747.
    • (2001) J. Cell Sci. , vol.114 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    Van Deurs, B.3    Sandvig, K.4
  • 128
    • 0023449563 scopus 로고
    • Ligands internalised through coated or non-coated invaginations follow a common intracellular pathway
    • Tran, D. J., Carpentier, J. L., Sawano, F., Gorden, P. and Orci, L., 1987, Ligands internalised through coated or non-coated invaginations follow a common intracellular pathway. Proc. Natl Acad. Sci. USA, 84, 7957-7961.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7957-7961
    • Tran, D.J.1    Carpentier, J.L.2    Sawano, F.3    Gorden, P.4    Orci, L.5
  • 130
    • 2942531984 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein caveolin chaperone complex. Involvement in cholesterol trafficking
    • Uittenbogaard, A., Ying, Y. S. and Smart, E. J., 1998, Characterization of a cytosolic heat-shock protein caveolin chaperone complex. Involvement in cholesterol trafficking. J. Biol. Chem., 275, 25595-25599.
    • (1998) J. Biol. Chem. , vol.275 , pp. 25595-25599
    • Uittenbogaard, A.1    Ying, Y.S.2    Smart, E.J.3
  • 132
    • 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
  • 134
    • 0034763783 scopus 로고    scopus 로고
    • Cholesterol does not induce segregation of liquid-ordered domains in bilayers modeling the inner leaflet of the plasma membrane
    • Wang, T. Y. and Silvius, J. R., 2001, Cholesterol does not induce segregation of liquid-ordered domains in bilayers modeling the inner leaflet of the plasma membrane. Biophys. J., 81, 2762-2773.
    • (2001) Biophys. J. , vol.81 , pp. 2762-2773
    • Wang, T.Y.1    Silvius, J.R.2
  • 135
    • 0033869609 scopus 로고    scopus 로고
    • Fluorescence-based evaluation of the partitioning of lipids and lipidated peptides into liquid-ordered microdomains: A model for molecular partitioning into 'lipid rafts'
    • Wang, T. Y., Leventis, R. and Silvius, J. R., 2000, Fluorescence-based evaluation of the partitioning of lipids and lipidated peptides into liquid-ordered microdomains: a model for molecular partitioning into 'lipid rafts'. Biophys. J., 79, 919-933.
    • (2000) Biophys. J. , vol.79 , pp. 919-933
    • Wang, T.Y.1    Leventis, R.2    Silvius, J.R.3
  • 136
    • 0035980238 scopus 로고    scopus 로고
    • Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes
    • Wang, T. Y., Leventis, R. and Silvius, J. R., 2001, Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes. Biochemistry, 40, 13031-13040.
    • (2001) Biochemistry , vol.40 , pp. 13031-13040
    • Wang, T.Y.1    Leventis, R.2    Silvius, J.R.3
  • 137
    • 0033082833 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation is localized within low-buoyant density, non-caveolar membrane domains
    • Waugh, M. G., Lawson, D. and Hsuann, J. J., 1999, Epidermal growth factor receptor activation is localized within low-buoyant density, non-caveolar membrane domains. Biochem. J., 337, 591-597.
    • (1999) Biochem. J. , vol.337 , pp. 591-597
    • Waugh, M.G.1    Lawson, D.2    Hsuann, J.J.3
  • 138
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., Brennan, T., Li, Q., McCormack, C. and Seed, B., 1998, Membrane compartmentation is required for efficient T cell activation. Immunity, 8, 723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 139
    • 0034620610 scopus 로고    scopus 로고
    • The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation
    • Xu, X. and London, E., 2000, The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation. Biochemistry, 39, 843-849.
    • (2000) Biochemistry , vol.39 , pp. 843-849
    • Xu, X.1    London, E.2
  • 140
    • 0037067715 scopus 로고    scopus 로고
    • Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts
    • Yamabhai, M. and Anderson, R. G. W., 2002, Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts. J. Biol. Chem., 277, 24843-24846.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24843-24846
    • Yamabhai, M.1    Anderson, R.G.W.2
  • 141
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epithelium of the mouse
    • Yamada, E., 1955, The fine structure of the gall bladder epithelium of the mouse. J. Biophys. Biochem. Cytol., 1, 445-458.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 445-458
    • Yamada, E.1
  • 142
    • 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
  • 143
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., Trible, R. P. and Samelson, L. E., 1998, LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity, 9, 239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.