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Volumn 72, Issue 1, 2009, Pages 12-22

Biochemical and proteomic approaches for the study of membrane microdomains

Author keywords

Membrane microdomain; Plasma membrane proteomics; Quantitative proteomics

Indexed keywords

CAVEOLIN; GLYCOSYLPHOSPHATIDYLINOSITOL; PHOSPHOLIPASE; PROTEOME; SILICON DIOXIDE; TETRASPANIN;

EID: 60649093057     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.09.003     Document Type: Review
Times cited : (40)

References (137)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., and von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 7 (1998) 1029-1038
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 2
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., and Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 175 (1972) 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 3
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson R.G., and Jacobson K. A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains. Science 296 (2002) 1821-1825
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2
  • 4
    • 0015147957 scopus 로고
    • The lipid class composition of Semliki forest virus and plasma membranes of the host cells
    • Renkonen O., Kaarainen L., Simons K., and Gahmberg C.G. The lipid class composition of Semliki forest virus and plasma membranes of the host cells. Virology 46 (1971) 318-326
    • (1971) Virology , vol.46 , pp. 318-326
    • Renkonen, O.1    Kaarainen, L.2    Simons, K.3    Gahmberg, C.G.4
  • 5
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits
    • Bhattacharyya R.P., Remenyi A., Yeh B.J., and Lim W.A. Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu Rev Biochem 75 (2006) 655-680
    • (2006) Annu Rev Biochem , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 7
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers
    • Dietrich C., Volovyk Z.N., Levi M., Thompson N.L., and Jacobson K. Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers. Proc Natl Acad Sci U S A 98 (2001) 10642-10647
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10642-10647
    • Dietrich, C.1    Volovyk, Z.N.2    Levi, M.3    Thompson, N.L.4    Jacobson, K.5
  • 9
    • 60649096913 scopus 로고    scopus 로고
    • Mass spectrometry outgrows simple biochemistry: new approaches to organelle proteomics
    • Foster L. Mass spectrometry outgrows simple biochemistry: new approaches to organelle proteomics. Biophys Rev Lett 1 (2006) 163-175
    • (2006) Biophys Rev Lett , vol.1 , pp. 163-175
    • Foster, L.1
  • 10
    • 34548286709 scopus 로고    scopus 로고
    • Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis
    • Rabilloud T., Luche S., Santoni V., and Chevallet M. Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis. Methods Mol Biol 355 (2007) 111-119
    • (2007) Methods Mol Biol , vol.355 , pp. 111-119
    • Rabilloud, T.1    Luche, S.2    Santoni, V.3    Chevallet, M.4
  • 11
    • 0037347236 scopus 로고    scopus 로고
    • Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis
    • Luche S., Santoni V., and Rabilloud T. Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis. Proteomics 3 (2003) 249-253
    • (2003) Proteomics , vol.3 , pp. 249-253
    • Luche, S.1    Santoni, V.2    Rabilloud, T.3
  • 12
    • 0036857488 scopus 로고    scopus 로고
    • Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry
    • Henningsen R., Gale B.L., Straub K.M., and DeNagel D.C. Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2 (2002) 1479-1488
    • (2002) Proteomics , vol.2 , pp. 1479-1488
    • Henningsen, R.1    Gale, B.L.2    Straub, K.M.3    DeNagel, D.C.4
  • 13
    • 45549110283 scopus 로고    scopus 로고
    • Overview of membrane protein solubilization
    • Chapter 5:Unit 5 9
    • Schimerlik M.I. Overview of membrane protein solubilization. Curr Protoc Neurosci (2001) Chapter 5:Unit 5 9
    • (2001) Curr Protoc Neurosci
    • Schimerlik, M.I.1
  • 14
    • 33750143252 scopus 로고    scopus 로고
    • Evaluation of the application of sodium deoxycholate to proteomic analysis of rat hippocampal plasma membrane
    • Zhou J., Zhou T., Cao R., Liu Z., Shen J., Chen P., et al. Evaluation of the application of sodium deoxycholate to proteomic analysis of rat hippocampal plasma membrane. J Proteome Res 5 (2006) 2547-2553
    • (2006) J Proteome Res , vol.5 , pp. 2547-2553
    • Zhou, J.1    Zhou, T.2    Cao, R.3    Liu, Z.4    Shen, J.5    Chen, P.6
  • 15
    • 0242291099 scopus 로고    scopus 로고
    • Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins
    • Yu Y.Q., Gilar M., Lee P.J., Bouvier E.S., and Gebler J.C. Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Anal Chem 75 (2003) 6023-6028
    • (2003) Anal Chem , vol.75 , pp. 6023-6028
    • Yu, Y.Q.1    Gilar, M.2    Lee, P.J.3    Bouvier, E.S.4    Gebler, J.C.5
  • 16
    • 39749125069 scopus 로고    scopus 로고
    • Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis
    • Masuda T., Tomita M., and Ishihama Y. Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis. J Proteome Res 7 (2008) 731-740
    • (2008) J Proteome Res , vol.7 , pp. 731-740
    • Masuda, T.1    Tomita, M.2    Ishihama, Y.3
  • 17
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • Husi H., Ward M.A., Choudhary J.S., Blackstock W.P., and Grant S.G. Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat Neurosci 3 (2000) 661-669
    • (2000) Nat Neurosci , vol.3 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.5
  • 18
    • 33646823604 scopus 로고    scopus 로고
    • Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome
    • Collins M.O., Husi H., Yu L., Brandon J.M., Anderson C.N., Blackstock W.P., et al. Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome. J Neurochem 97 Suppl 1 (2006) 16-23
    • (2006) J Neurochem , vol.97 , Issue.SUPPL. 1 , pp. 16-23
    • Collins, M.O.1    Husi, H.2    Yu, L.3    Brandon, J.M.4    Anderson, C.N.5    Blackstock, W.P.6
  • 19
    • 0035910607 scopus 로고    scopus 로고
    • Functional proteomic analysis of protein kinase C epsilon signaling complexes in the normal heart and during cardioprotection
    • Ping P., Zhang J., Pierce Jr. W.M., and Bolli R. Functional proteomic analysis of protein kinase C epsilon signaling complexes in the normal heart and during cardioprotection. Circ Res 88 (2001) 59-62
    • (2001) Circ Res , vol.88 , pp. 59-62
    • Ping, P.1    Zhang, J.2    Pierce Jr., W.M.3    Bolli, R.4
  • 20
    • 42149120753 scopus 로고    scopus 로고
    • Immunoproteomic discovery of novel T cell antigens from the obligate intracellular pathogen Chlamydia
    • Karunakaran K.P., Rey-Ladino J., Stoynov N., Berg K., Shen C., Jiang X., et al. Immunoproteomic discovery of novel T cell antigens from the obligate intracellular pathogen Chlamydia. J Immunol 180 (2008) 2459-2465
    • (2008) J Immunol , vol.180 , pp. 2459-2465
    • Karunakaran, K.P.1    Rey-Ladino, J.2    Stoynov, N.3    Berg, K.4    Shen, C.5    Jiang, X.6
  • 21
    • 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. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci U S A 100 (2003) 5813-5818
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 22
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 23
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., and Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68 (1992) 533-544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 24
    • 0037388897 scopus 로고    scopus 로고
    • Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation
    • Li N., Mak A., Richards D.P., Naber C., Keller B.O., Li L., et al. Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation. Proteomics 3 (2003) 536-548
    • (2003) Proteomics , vol.3 , pp. 536-548
    • Li, N.1    Mak, A.2    Richards, D.P.3    Naber, C.4    Keller, B.O.5    Li, L.6
  • 25
    • 50949133928 scopus 로고    scopus 로고
    • Francisella targets cholesterol-rich host cell membrane domains for entry into macrophages
    • Tamilselvam B., and Daefler S. Francisella targets cholesterol-rich host cell membrane domains for entry into macrophages. J Immunol 180 (2008) 8262-8271
    • (2008) J Immunol , vol.180 , pp. 8262-8271
    • Tamilselvam, B.1    Daefler, S.2
  • 26
    • 19044381573 scopus 로고    scopus 로고
    • Interferon gamma induces translocation of commensal Escherichia coli across gut epithelial cells via a lipid raft-mediated process
    • Clark E., Hoare C., Tanianis-Hughes J., Carlson G.L., and Warhurst G. Interferon gamma induces translocation of commensal Escherichia coli across gut epithelial cells via a lipid raft-mediated process. Gastroenterology 128 (2005) 1258-1267
    • (2005) Gastroenterology , vol.128 , pp. 1258-1267
    • Clark, E.1    Hoare, C.2    Tanianis-Hughes, J.3    Carlson, G.L.4    Warhurst, G.5
  • 27
    • 0037530035 scopus 로고    scopus 로고
    • Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells
    • Stuart E.S., Webley W.C., and Norkin L.C. Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells. Exp Cell Res 287 (2003) 67-78
    • (2003) Exp Cell Res , vol.287 , pp. 67-78
    • Stuart, E.S.1    Webley, W.C.2    Norkin, L.C.3
  • 28
    • 51449121120 scopus 로고    scopus 로고
    • Lipid raft-dependent uptake, signaling, and intracellular fate of Porphyromonas gingivalis in mouse macrophages
    • Wang M., and Hajishengallis G. Lipid raft-dependent uptake, signaling, and intracellular fate of Porphyromonas gingivalis in mouse macrophages. Cell Microbiol 10 (2008) 2029-2042
    • (2008) Cell Microbiol , vol.10 , pp. 2029-2042
    • Wang, M.1    Hajishengallis, G.2
  • 29
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K., and van Meer G. Lipid sorting in epithelial cells. Biochemistry 27 (1988) 6197-6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    van Meer, G.2
  • 30
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder R., London E., and Brown D. Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc Natl Acad Sci U S A 91 (1994) 12130-12134
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 31
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown D.A., and London E. Structure and origin of ordered lipid domains in biological membranes. J Membr Biol 164 (1998) 103-114
    • (1998) J Membr Biol , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 32
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • Schroeder R.J., Ahmed S.N., Zhu Y., London E., and Brown D.A. Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains. J Biol Chem 273 (1998) 1150-1157
    • (1998) J Biol Chem , vol.273 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 33
    • 0037135518 scopus 로고    scopus 로고
    • Sphingolipid transport: rafts and translocators
    • van Meer G., and Lisman Q. Sphingolipid transport: rafts and translocators. J Biol Chem 277 (2002) 25855-25858
    • (2002) J Biol Chem , vol.277 , pp. 25855-25858
    • van Meer, G.1    Lisman, Q.2
  • 34
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function
    • Pike L.J. Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function. J Lipid Res 47 (2006) 1597-1598
    • (2006) J Lipid Res , vol.47 , pp. 1597-1598
    • Pike, L.J.1
  • 35
    • 0038492661 scopus 로고    scopus 로고
    • Dynamic, yet structured: the cell membrane three decades after the Singer-Nicolson model
    • Vereb G., Szollosi J., Matko J., Nagy P., Farkas T., Vigh L., et al. Dynamic, yet structured: the cell membrane three decades after the Singer-Nicolson model. Proc Natl Acad Sci U S A 100 (2003) 8053-8058
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8053-8058
    • Vereb, G.1    Szollosi, J.2    Matko, J.3    Nagy, P.4    Farkas, T.5    Vigh, L.6
  • 36
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H. Triton promotes domain formation in lipid raft mixtures. Biophys J 83 (2002) 2693-2701
    • (2002) Biophys J , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 37
    • 0038730762 scopus 로고    scopus 로고
    • The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton
    • Heerklotz H., Szadkowska H., Anderson T., and Seelig J. The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton. J Mol Biol 329 (2003) 793-799
    • (2003) J Mol Biol , vol.329 , pp. 793-799
    • Heerklotz, H.1    Szadkowska, H.2    Anderson, T.3    Seelig, J.4
  • 38
    • 11144344415 scopus 로고    scopus 로고
    • Membrane redistribution of gangliosides and glycosylphosphatidylinositol-anchored proteins in brain tissue sections under conditions of lipid raft isolation
    • Heffer-Lauc M., Lauc G., Nimrichter L., Fromholt S.E., and Schnaar R.L. Membrane redistribution of gangliosides and glycosylphosphatidylinositol-anchored proteins in brain tissue sections under conditions of lipid raft isolation. Biochim Biophys Acta 1686 3 (2005) 200-208
    • (2005) Biochim Biophys Acta , vol.1686 , Issue.3 , pp. 200-208
    • Heffer-Lauc, M.1    Lauc, G.2    Nimrichter, L.3    Fromholt, S.E.4    Schnaar, R.L.5
  • 39
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid/cholesterol-rich detergent-insoluble 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. On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes. Biochemistry 36 (1997) 10944-10953
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 40
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T., and Kurzchalia T.V. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394 (1998) 802-805
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 41
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., and Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394 (1998) 798-801
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 42
    • 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. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J Cell Biol 148 (2000) 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
  • 43
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., and Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol 141 (1998) 929-942
    • (1998) J Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 44
    • 38949168914 scopus 로고    scopus 로고
    • Visualization of detergent solubilization of membranes: implications for the isolation of rafts
    • Garner A.E., Smith D.A., and Hooper N.M. Visualization of detergent solubilization of membranes: implications for the isolation of rafts. Biophys J 94 (2008) 1326-1340
    • (2008) Biophys J , vol.94 , pp. 1326-1340
    • Garner, A.E.1    Smith, D.A.2    Hooper, N.M.3
  • 45
    • 0347298692 scopus 로고    scopus 로고
    • Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering
    • Bini L., Pacini S., Liberatori S., Valensin S., Pellegrini M., Raggiaschi R., et al. Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering. Biochem J 369 (2003) 301-309
    • (2003) Biochem J , vol.369 , pp. 301-309
    • Bini, L.1    Pacini, S.2    Liberatori, S.3    Valensin, S.4    Pellegrini, M.5    Raggiaschi, R.6
  • 46
    • 32344443165 scopus 로고    scopus 로고
    • Combined chemical and enzymatic stable isotope labeling for quantitative profiling of detergent-insoluble membrane proteins isolated using Triton X-100 and Brij-96
    • Blonder J., Yu L.R., Radeva G., Chan K.C., Lucas D.A., Waybright T.J., et al. Combined chemical and enzymatic stable isotope labeling for quantitative profiling of detergent-insoluble membrane proteins isolated using Triton X-100 and Brij-96. J Proteome Res 5 (2006) 349-360
    • (2006) J Proteome Res , vol.5 , pp. 349-360
    • Blonder, J.1    Yu, L.R.2    Radeva, G.3    Chan, K.C.4    Lucas, D.A.5    Waybright, T.J.6
  • 47
    • 13244292296 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the glycosphingolipid-enriched microdomains of rat natural killer cells
    • Man P., Novak P., Cebecauer M., Horvath O., Fiserova A., Havlicek V., et al. Mass spectrometric analysis of the glycosphingolipid-enriched microdomains of rat natural killer cells. Proteomics 5 (2005) 113-122
    • (2005) Proteomics , vol.5 , pp. 113-122
    • Man, P.1    Novak, P.2    Cebecauer, M.3    Horvath, O.4    Fiserova, A.5    Havlicek, V.6
  • 49
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins
    • Song K.S., Scherer P.E., Tang Z., Okamoto T., Li S., Chafel M., et al. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J Biol Chem 271 (1996) 15160-15165
    • (1996) J Biol Chem , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.3    Okamoto, T.4    Li, S.5    Chafel, M.6
  • 50
    • 22244469306 scopus 로고    scopus 로고
    • A simplified method for the preparation of detergent-free lipid rafts
    • Macdonald J.L., and Pike L.J. A simplified method for the preparation of detergent-free lipid rafts. J Lipid Res 46 (2005) 1061-1067
    • (2005) J Lipid Res , vol.46 , pp. 1061-1067
    • Macdonald, J.L.1    Pike, L.J.2
  • 51
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart E.J., Ying Y.S., Mineo C., and Anderson R.G. A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc Natl Acad Sci U S A 92 (1995) 10104-10108
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 52
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1 (2002) 376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 53
    • 0030695849 scopus 로고    scopus 로고
    • Use of cyclodextrins for manipulating cellular cholesterol content
    • Christian A.E., Haynes M.P., Phillips M.C., and Rothblat G.H. Use of cyclodextrins for manipulating cellular cholesterol content. J Lipid Res 38 (1997) 2264-2272
    • (1997) J Lipid Res , vol.38 , pp. 2264-2272
    • Christian, A.E.1    Haynes, M.P.2    Phillips, M.C.3    Rothblat, G.H.4
  • 54
    • 0032532271 scopus 로고    scopus 로고
    • Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
    • Ilangumaran S., and Hoessli D.C. Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane. Biochem J 335 Pt 2 (1998) 433-440
    • (1998) Biochem J , vol.335 , Issue.PART 2 , pp. 433-440
    • Ilangumaran, S.1    Hoessli, D.C.2
  • 55
    • 8744293655 scopus 로고    scopus 로고
    • Lipid raft proteome reveals ATP synthase complex in the cell surface
    • Bae T.J., Kim M.S., Kim J.W., Kim B.W., Choo H.J., Lee J.W., et al. Lipid raft proteome reveals ATP synthase complex in the cell surface. Proteomics 4 (2004) 3536-3548
    • (2004) Proteomics , vol.4 , pp. 3536-3548
    • Bae, T.J.1    Kim, M.S.2    Kim, J.W.3    Kim, B.W.4    Choo, H.J.5    Lee, J.W.6
  • 56
    • 31344468377 scopus 로고    scopus 로고
    • Detergent-free caveolae proteome suggests an interaction with ER and mitochondria
    • McMahon K.A., Zhu M., Kwon S.W., Liu P., Zhao Y., and Anderson R.G. Detergent-free caveolae proteome suggests an interaction with ER and mitochondria. Proteomics 6 (2006) 143-152
    • (2006) Proteomics , vol.6 , pp. 143-152
    • McMahon, K.A.1    Zhu, M.2    Kwon, S.W.3    Liu, P.4    Zhao, Y.5    Anderson, R.G.6
  • 57
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T., and Simons K. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr Opin Cell Biol 9 (1997) 534-542
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 58
    • 29144534595 scopus 로고    scopus 로고
    • Structure of caveolae
    • Stan R.V. Structure of caveolae. Biochim Biophys Acta 1746 (2005) 334-348
    • (2005) Biochim Biophys Acta , vol.1746 , pp. 334-348
    • Stan, R.V.1
  • 59
    • 0020645545 scopus 로고
    • Morphological changes of the 3T3-L1 fibroblast plasma membrane upon differentiation to the adipocyte form
    • Fan J.Y., Carpentier J.L., van Obberghen E., Grunfeld C., Gorden P., and Orci L. Morphological changes of the 3T3-L1 fibroblast plasma membrane upon differentiation to the adipocyte form. J Cell Sci 61 (1983) 219-230
    • (1983) J Cell Sci , vol.61 , pp. 219-230
    • Fan, J.Y.1    Carpentier, J.L.2    van Obberghen, E.3    Grunfeld, C.4    Gorden, P.5    Orci, L.6
  • 60
    • 48649089133 scopus 로고    scopus 로고
    • Detergent-resistant membrane subfractions containing proteins of plasma membrane, mitochondrial, and internal membrane origins
    • Mellgren R.L. Detergent-resistant membrane subfractions containing proteins of plasma membrane, mitochondrial, and internal membrane origins. J Biochem Biophys Methods 70 (2008) 1029-1036
    • (2008) J Biochem Biophys Methods , vol.70 , pp. 1029-1036
    • Mellgren, R.L.1
  • 61
    • 0035964954 scopus 로고    scopus 로고
    • Loss of caveolae, vascular dysfunction, and pulmonary defects in caveolin-1 gene-disrupted mice
    • Drab M., Verkade P., Elger M., Kasper M., Lohn M., Lauterbach B., et al. Loss of caveolae, vascular dysfunction, and pulmonary defects in caveolin-1 gene-disrupted mice. Science 293 (2001) 2449-2452
    • (2001) Science , vol.293 , pp. 2449-2452
    • Drab, M.1    Verkade, P.2    Elger, M.3    Kasper, M.4    Lohn, M.5    Lauterbach, B.6
  • 62
    • 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., et al. 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 (2001) 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
  • 63
    • 0030222108 scopus 로고    scopus 로고
    • Caveolae and caveolins
    • Parton R.G. Caveolae and caveolins. Curr Opin Cell Biol 8 (1996) 542-548
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 542-548
    • Parton, R.G.1
  • 64
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane
    • Okamoto T., Schlegel A., Scherer P.E., and Lisanti M.P. Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane. J Biol Chem 273 (1998) 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
  • 66
    • 14444285478 scopus 로고    scopus 로고
    • Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo
    • Scherer P.E., Lewis R.Y., Volonte D., Engelman J.A., Galbiati F., Couet J., et al. Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo. J Biol Chem 272 (1997) 29337-29346
    • (1997) J Biol Chem , vol.272 , pp. 29337-29346
    • Scherer, P.E.1    Lewis, R.Y.2    Volonte, D.3    Engelman, J.A.4    Galbiati, F.5    Couet, J.6
  • 67
    • 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. VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro. Mol Biol Cell 6 (1995) 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
  • 70
    • 0033529643 scopus 로고    scopus 로고
    • A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro
    • Schlegel A., Schwab R.B., Scherer P.E., and Lisanti M.P. A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro. J Biol Chem 274 (1999) 22660-22667
    • (1999) J Biol Chem , vol.274 , pp. 22660-22667
    • Schlegel, A.1    Schwab, R.B.2    Scherer, P.E.3    Lisanti, M.P.4
  • 71
    • 0034647940 scopus 로고    scopus 로고
    • A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo
    • Schlegel A., and Lisanti M.P. A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo. J Biol Chem 275 (2000) 21605-21617
    • (2000) J Biol Chem , vol.275 , pp. 21605-21617
    • Schlegel, A.1    Lisanti, M.P.2
  • 72
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • Couet J., Li S., Okamoto T., Ikezu T., and Lisanti M.P. Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J Biol Chem 272 (1997) 6525-6533
    • (1997) J Biol Chem , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 73
    • 0028319060 scopus 로고
    • Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease
    • Lisanti M.P., Scherer P.E., Vidugiriene J., Tang Z., Hermanowski-Vosatka A., Tu Y.H., et al. Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease. J Cell Biol 126 (1994) 111-126
    • (1994) J Cell Biol , vol.126 , pp. 111-126
    • Lisanti, M.P.1    Scherer, P.E.2    Vidugiriene, J.3    Tang, Z.4    Hermanowski-Vosatka, A.5    Tu, Y.H.6
  • 74
    • 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. Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 122 (1993) 789-807
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 76
  • 77
    • 0037663884 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue
    • Cohen A.W., Razani B., Wang X.B., Combs T.P., Williams T.M., Scherer P.E., et al. Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue. Am J Physiol Cell Physiol 285 (2003) C222-235
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Cohen, A.W.1    Razani, B.2    Wang, X.B.3    Combs, T.P.4    Williams, T.M.5    Scherer, P.E.6
  • 79
    • 0033306884 scopus 로고    scopus 로고
    • Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells
    • Nystrom F.H., Chen H., Cong L.N., Li Y., and Quon M.J. Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells. Mol Endocrinol 13 (1999) 2013-2024
    • (1999) Mol Endocrinol , vol.13 , pp. 2013-2024
    • Nystrom, F.H.1    Chen, H.2    Cong, L.N.3    Li, Y.4    Quon, M.J.5
  • 81
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L., Puntener D., and Helenius A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296 (2002) 535-539
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 82
    • 0033540271 scopus 로고    scopus 로고
    • Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae
    • Chen Y., and Norkin L.C. Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae. Exp Cell Res 246 (1999) 83-90
    • (1999) Exp Cell Res , vol.246 , pp. 83-90
    • Chen, Y.1    Norkin, L.C.2
  • 84
    • 0035866759 scopus 로고    scopus 로고
    • Invasion activating caveolin-1 mutation in human scirrhous breast cancers
    • Hayashi K., Matsuda S., Machida K., Yamamoto T., Fukuda Y., Nimura Y., et al. Invasion activating caveolin-1 mutation in human scirrhous breast cancers. Cancer Res 61 (2001) 2361-2364
    • (2001) Cancer Res , vol.61 , pp. 2361-2364
    • Hayashi, K.1    Matsuda, S.2    Machida, K.3    Yamamoto, T.4    Fukuda, Y.5    Nimura, Y.6
  • 85
    • 0036791604 scopus 로고    scopus 로고
    • Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia
    • Lee H., Park D.S., Razani B., Russell R.G., Pestell R.G., and Lisanti M.P. Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia. Am J Pathol 161 (2002) 1357-1369
    • (2002) Am J Pathol , vol.161 , pp. 1357-1369
    • Lee, H.1    Park, D.S.2    Razani, B.3    Russell, R.G.4    Pestell, R.G.5    Lisanti, M.P.6
  • 86
    • 4544299036 scopus 로고    scopus 로고
    • Identification of caveolae and their signature proteins caveolin 1 and 2 in the lens
    • Lo W.K., Zhou C.J., and Reddan J. Identification of caveolae and their signature proteins caveolin 1 and 2 in the lens. Exp Eye Res 79 (2004) 487-498
    • (2004) Exp Eye Res , vol.79 , pp. 487-498
    • Lo, W.K.1    Zhou, C.J.2    Reddan, J.3
  • 88
    • 33645464380 scopus 로고    scopus 로고
    • Proteomic analysis of membrane microdomains derived from both failing and non-failing human hearts
    • Banfi C., Brioschi M., Wait R., Begum S., Gianazza E., Fratto P., et al. Proteomic analysis of membrane microdomains derived from both failing and non-failing human hearts. Proteomics 6 (2006) 1976-1988
    • (2006) Proteomics , vol.6 , pp. 1976-1988
    • Banfi, C.1    Brioschi, M.2    Wait, R.3    Begum, S.4    Gianazza, E.5    Fratto, P.6
  • 89
    • 45549107278 scopus 로고    scopus 로고
    • Compartmentalisation of cAMP-dependent signalling by caveolae in the adult cardiac myocyte
    • Calaghan S., Kozera L., and White E. Compartmentalisation of cAMP-dependent signalling by caveolae in the adult cardiac myocyte. J Mol Cell Cardiol 45 (2008) 88-92
    • (2008) J Mol Cell Cardiol , vol.45 , pp. 88-92
    • Calaghan, S.1    Kozera, L.2    White, E.3
  • 90
    • 33845938227 scopus 로고    scopus 로고
    • Cholesterol reduction by methyl-beta-cyclodextrin attenuates the delta opioid receptor-mediated signaling in neuronal cells but enhances it in non-neuronal cells
    • Huang P., Xu W., Yoon S.I., Chen C., Chong P.L., and Liu-Chen L.Y. Cholesterol reduction by methyl-beta-cyclodextrin attenuates the delta opioid receptor-mediated signaling in neuronal cells but enhances it in non-neuronal cells. Biochem Pharmacol 73 (2007) 534-549
    • (2007) Biochem Pharmacol , vol.73 , pp. 534-549
    • Huang, P.1    Xu, W.2    Yoon, S.I.3    Chen, C.4    Chong, P.L.5    Liu-Chen, L.Y.6
  • 91
    • 0021112527 scopus 로고
    • Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins
    • Chaney L.K., and Jacobson B.S. Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins. J Biol Chem 258 (1983) 10062-10072
    • (1983) J Biol Chem , vol.258 , pp. 10062-10072
    • Chaney, L.K.1    Jacobson, B.S.2
  • 92
    • 0028925762 scopus 로고
    • Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor
    • Schnitzer J.E., Oh P., Jacobson B.S., and Dvorak A.M. Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor. Proc Natl Acad Sci U S A 92 (1995) 1759-1763
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1759-1763
    • Schnitzer, J.E.1    Oh, P.2    Jacobson, B.S.3    Dvorak, A.M.4
  • 93
    • 0033551731 scopus 로고    scopus 로고
    • Immunoisolation of caveolae with high affinity antibody binding to the oligomeric caveolin cage. Toward understanding the basis of purification
    • Oh P., and Schnitzer J.E. Immunoisolation of caveolae with high affinity antibody binding to the oligomeric caveolin cage. Toward understanding the basis of purification. J Biol Chem 274 (1999) 23144-23154
    • (1999) J Biol Chem , vol.274 , pp. 23144-23154
    • Oh, P.1    Schnitzer, J.E.2
  • 94
    • 1842376838 scopus 로고    scopus 로고
    • Immunoisolation and partial characterization of endothelial plasmalemmal vesicles (caveolae)
    • Stan R.V., Roberts W.G., Predescu D., Ihida K., Saucan L., Ghitescu L., et al. Immunoisolation and partial characterization of endothelial plasmalemmal vesicles (caveolae). Mol Biol Cell 8 (1997) 595-605
    • (1997) Mol Biol Cell , vol.8 , pp. 595-605
    • Stan, R.V.1    Roberts, W.G.2    Predescu, D.3    Ihida, K.4    Saucan, L.5    Ghitescu, L.6
  • 95
    • 37649011760 scopus 로고    scopus 로고
    • PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and function
    • Hill M.M., Bastiani M., Luetterforst R., Kirkham M., Kirkham A., Nixon S.J., et al. PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and function. Cell 132 (2008) 113-124
    • (2008) Cell , vol.132 , pp. 113-124
    • Hill, M.M.1    Bastiani, M.2    Luetterforst, R.3    Kirkham, M.4    Kirkham, A.5    Nixon, S.J.6
  • 97
    • 0030947554 scopus 로고    scopus 로고
    • The tetraspanin superfamily: molecular facilitators
    • Maecker H.T., Todd S.C., and Levy S. The tetraspanin superfamily: molecular facilitators. FASEB J 11 (1997) 428-442
    • (1997) FASEB J , vol.11 , pp. 428-442
    • Maecker, H.T.1    Todd, S.C.2    Levy, S.3
  • 98
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immune-signalling complexes
    • Levy S., and Shoham T. The tetraspanin web modulates immune-signalling complexes. Nat Rev Immunol 5 (2005) 136-148
    • (2005) Nat Rev Immunol , vol.5 , pp. 136-148
    • Levy, S.1    Shoham, T.2
  • 99
    • 0031895778 scopus 로고    scopus 로고
    • CD81 (TAPA-1): a molecule involved in signal transduction and cell adhesion in the immune system
    • Levy S., Todd S.C., and Maecker H.T. CD81 (TAPA-1): a molecule involved in signal transduction and cell adhesion in the immune system. Annu Rev Immunol 16 (1998) 89-109
    • (1998) Annu Rev Immunol , vol.16 , pp. 89-109
    • Levy, S.1    Todd, S.C.2    Maecker, H.T.3
  • 100
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: more than meets the eye
    • Berditchevski F. Complexes of tetraspanins with integrins: more than meets the eye. J Cell Sci 114 (2001) 4143-4151
    • (2001) J Cell Sci , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 101
    • 0037234454 scopus 로고    scopus 로고
    • Hepatocyte CD81 is required for Plasmodium falciparum and Plasmodium yoelii sporozoite infectivity
    • Silvie O., Rubinstein E., Franetich J.F., Prenant M., Belnoue E., Renia L., et al. Hepatocyte CD81 is required for Plasmodium falciparum and Plasmodium yoelii sporozoite infectivity. Nat Med 9 (2003) 93-96
    • (2003) Nat Med , vol.9 , pp. 93-96
    • Silvie, O.1    Rubinstein, E.2    Franetich, J.F.3    Prenant, M.4    Belnoue, E.5    Renia, L.6
  • 102
    • 0033968407 scopus 로고    scopus 로고
    • A new gene involved in X-linked mental retardation identified by analysis of an X;2 balanced translocation
    • Zemni R., Bienvenu T., Vinet M.C., Sefiani A., Carrie A., Billuart P., et al. A new gene involved in X-linked mental retardation identified by analysis of an X;2 balanced translocation. Nat Genet 24 (2000) 167-170
    • (2000) Nat Genet , vol.24 , pp. 167-170
    • Zemni, R.1    Bienvenu, T.2    Vinet, M.C.3    Sefiani, A.4    Carrie, A.5    Billuart, P.6
  • 104
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts
    • Claas C., Stipp C.S., and Hemler M.E. Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts. J Biol Chem 276 (2001) 7974-7984
    • (2001) J Biol Chem , vol.276 , pp. 7974-7984
    • Claas, C.1    Stipp, C.S.2    Hemler, M.E.3
  • 105
    • 36049017470 scopus 로고    scopus 로고
    • Platelet tetraspanin complexes and their association with lipid rafts
    • Israels S.J., and McMillan-Ward E.M. Platelet tetraspanin complexes and their association with lipid rafts. Thromb Haemost 98 (2007) 1081-1087
    • (2007) Thromb Haemost , vol.98 , pp. 1081-1087
    • Israels, S.J.1    McMillan-Ward, E.M.2
  • 106
    • 0030062129 scopus 로고    scopus 로고
    • Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM proteins)
    • Berditchevski F., Zutter M.M., and Hemler M.E. Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM proteins). Mol Biol Cell 7 (1996) 193-207
    • (1996) Mol Biol Cell , vol.7 , pp. 193-207
    • Berditchevski, F.1    Zutter, M.M.2    Hemler, M.E.3
  • 107
    • 10244261559 scopus 로고    scopus 로고
    • CD9, CD63, CD81, and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins
    • Rubinstein E., Le Naour F., Lagaudriere-Gesbert C., Billard M., Conjeaud H., and Boucheix C. CD9, CD63, CD81, and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins. Eur J Immunol 26 (1996) 2657-2665
    • (1996) Eur J Immunol , vol.26 , pp. 2657-2665
    • Rubinstein, E.1    Le Naour, F.2    Lagaudriere-Gesbert, C.3    Billard, M.4    Conjeaud, H.5    Boucheix, C.6
  • 108
    • 1542267725 scopus 로고    scopus 로고
    • Tetraspanins connect several types of Ig proteins: IgM is a novel component of the tetraspanin web on B-lymphoid cells
    • Le Naour F., Charrin S., Labas V., Le Caer J.P., Boucheix C., and Rubinstein E. Tetraspanins connect several types of Ig proteins: IgM is a novel component of the tetraspanin web on B-lymphoid cells. Cancer Immunol Immunother 53 (2004) 148-152
    • (2004) Cancer Immunol Immunother , vol.53 , pp. 148-152
    • Le Naour, F.1    Charrin, S.2    Labas, V.3    Le Caer, J.P.4    Boucheix, C.5    Rubinstein, E.6
  • 109
    • 0035895876 scopus 로고    scopus 로고
    • FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
    • Stipp C.S., Orlicky D., and Hemler M.E. FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein. J Biol Chem 276 (2001) 4853-4862
    • (2001) J Biol Chem , vol.276 , pp. 4853-4862
    • Stipp, C.S.1    Orlicky, D.2    Hemler, M.E.3
  • 110
    • 0035500912 scopus 로고    scopus 로고
    • PGRL is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins
    • Clark K.L., Zeng Z., Langford A.L., Bowen S.M., and Todd S.C. PGRL is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins. J Immunol 167 (2001) 5115-5121
    • (2001) J Immunol , vol.167 , pp. 5115-5121
    • Clark, K.L.1    Zeng, Z.2    Langford, A.L.3    Bowen, S.M.4    Todd, S.C.5
  • 111
    • 0023883979 scopus 로고
    • Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane
    • Ferguson M.A., Homans S.W., Dwek R.A., and Rademacher T.W. Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane. Science 239 (1988) 753-759
    • (1988) Science , vol.239 , pp. 753-759
    • Ferguson, M.A.1    Homans, S.W.2    Dwek, R.A.3    Rademacher, T.W.4
  • 112
    • 0035376717 scopus 로고    scopus 로고
    • Determination of glycosyl-phosphatidylinositol membrane protein anchorage
    • Hooper N.M. Determination of glycosyl-phosphatidylinositol membrane protein anchorage. Proteomics 1 (2001) 748-755
    • (2001) Proteomics , vol.1 , pp. 748-755
    • Hooper, N.M.1
  • 113
    • 0036606913 scopus 로고    scopus 로고
    • Lipopolysaccharide recognition: CD14, TLRs and the LPS-activation cluster
    • Triantafilou M., and Triantafilou K. Lipopolysaccharide recognition: CD14, TLRs and the LPS-activation cluster. Trends Immunol 23 (2002) 301-304
    • (2002) Trends Immunol , vol.23 , pp. 301-304
    • Triantafilou, M.1    Triantafilou, K.2
  • 114
    • 0034746376 scopus 로고    scopus 로고
    • Released GFRalpha1 potentiates downstream signaling, neuronal survival, and differentiation via a novel mechanism of recruitment of c-Ret to lipid rafts
    • Paratcha G., Ledda F., Baars L., Coulpier M., Besset V., Anders J., et al. Released GFRalpha1 potentiates downstream signaling, neuronal survival, and differentiation via a novel mechanism of recruitment of c-Ret to lipid rafts. Neuron 29 (2001) 171-184
    • (2001) Neuron , vol.29 , pp. 171-184
    • Paratcha, G.1    Ledda, F.2    Baars, L.3    Coulpier, M.4    Besset, V.5    Anders, J.6
  • 116
    • 33645290776 scopus 로고    scopus 로고
    • The prion protein and lipid rafts
    • Taylor D.R., and Hooper N.M. The prion protein and lipid rafts. Mol Membr Biol 23 (2006) 89-99
    • (2006) Mol Membr Biol , vol.23 , pp. 89-99
    • Taylor, D.R.1    Hooper, N.M.2
  • 117
    • 0037449769 scopus 로고    scopus 로고
    • Glucosamine inhibits inositol acylation of the glycosylphosphatidylinositol anchors in intraerythrocytic Plasmodium falciparum
    • Naik R.S., Krishnegowda G., and Gowda D.C. Glucosamine inhibits inositol acylation of the glycosylphosphatidylinositol anchors in intraerythrocytic Plasmodium falciparum. J Biol Chem 278 (2003) 2036-2042
    • (2003) J Biol Chem , vol.278 , pp. 2036-2042
    • Naik, R.S.1    Krishnegowda, G.2    Gowda, D.C.3
  • 119
  • 120
    • 41449098351 scopus 로고    scopus 로고
    • Targeted drug delivery via folate receptors
    • Zhao X., Li H., and Lee R.J. Targeted drug delivery via folate receptors. Expert Opin Drug Deliv 5 (2008) 309-319
    • (2008) Expert Opin Drug Deliv , vol.5 , pp. 309-319
    • Zhao, X.1    Li, H.2    Lee, R.J.3
  • 121
    • 60649090007 scopus 로고    scopus 로고
    • D.B. Kronegg, D., 1999, http://www.expasy.ch/tools.
    • D.B. Kronegg, D., 1999, http://www.expasy.ch/tools.
  • 122
    • 0035049164 scopus 로고    scopus 로고
    • Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes
    • Eisenhaber B., Bork P., and Eisenhaber F. Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes. Protein Eng 14 (2001) 17-25
    • (2001) Protein Eng , vol.14 , pp. 17-25
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 123
    • 18744414791 scopus 로고    scopus 로고
    • Identification of GPI anchor attachment signals by a Kohonen self-organizing map
    • Fankhauser N., and Maser P. Identification of GPI anchor attachment signals by a Kohonen self-organizing map. Bioinformatics 21 (2005) 1846-1852
    • (2005) Bioinformatics , vol.21 , pp. 1846-1852
    • Fankhauser, N.1    Maser, P.2
  • 124
    • 34347373519 scopus 로고    scopus 로고
    • Computational approach for identification and characterization of GPI-anchored peptides in proteomics experiments
    • Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K., Arizmendi J.M., Jensen O.N., et al. Computational approach for identification and characterization of GPI-anchored peptides in proteomics experiments. Proteomics 7 (2007) 1951-1960
    • (2007) Proteomics , vol.7 , pp. 1951-1960
    • Omaetxebarria, M.J.1    Elortza, F.2    Rodriguez-Suarez, E.3    Aloria, K.4    Arizmendi, J.M.5    Jensen, O.N.6
  • 125
    • 0042164911 scopus 로고    scopus 로고
    • Enhanced resolution of glycosylphosphatidylinositol-anchored and transmembrane proteins from the lipid-rich myelin membrane by two-dimensional gel electrophoresis
    • Taylor C.M., and Pfeiffer S.E. Enhanced resolution of glycosylphosphatidylinositol-anchored and transmembrane proteins from the lipid-rich myelin membrane by two-dimensional gel electrophoresis. Proteomics 3 (2003) 1303-1312
    • (2003) Proteomics , vol.3 , pp. 1303-1312
    • Taylor, C.M.1    Pfeiffer, S.E.2
  • 126
    • 0023269198 scopus 로고
    • Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C
    • Hooper N.M., Low M.G., and Turner A.J. Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C. Biochem J 244 (1987) 465-469
    • (1987) Biochem J , vol.244 , pp. 465-469
    • Hooper, N.M.1    Low, M.G.2    Turner, A.J.3
  • 127
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem 256 (1981) 1604-1607
    • (1981) J Biol Chem , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 128
    • 0029904799 scopus 로고    scopus 로고
    • Isolation and characterization of two distinct low-density, Triton-insoluble, complexes from porcine lung membranes
    • Parkin E.T., Turner A.J., and Hooper N.M. Isolation and characterization of two distinct low-density, Triton-insoluble, complexes from porcine lung membranes. Biochem J 319 Pt 3 (1996) 887-896
    • (1996) Biochem J , vol.319 , Issue.PART 3 , pp. 887-896
    • Parkin, E.T.1    Turner, A.J.2    Hooper, N.M.3
  • 129
    • 0141958827 scopus 로고    scopus 로고
    • Identification of novel Bacillus thuringiensis Cry1Ac binding proteins in Manduca sexta midgut through proteomic analysis
    • McNall R.J., and Adang M.J. Identification of novel Bacillus thuringiensis Cry1Ac binding proteins in Manduca sexta midgut through proteomic analysis. Insect Biochem Mol Biol 33 (2003) 999-1010
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 999-1010
    • McNall, R.J.1    Adang, M.J.2
  • 131
    • 33645795446 scopus 로고    scopus 로고
    • Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment
    • Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuhse T.S., Brodbeck U., et al. Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment. J Proteome Res 5 (2006) 935-943
    • (2006) J Proteome Res , vol.5 , pp. 935-943
    • Elortza, F.1    Mohammed, S.2    Bunkenborg, J.3    Foster, L.J.4    Nuhse, T.S.5    Brodbeck, U.6
  • 132
    • 35648988480 scopus 로고    scopus 로고
    • Quantifying raft proteins in neonatal mouse brain by 'tube-gel' protein digestion label-free shotgun proteomics
    • Yu H., Wakim B., Li M., Halligan B., Tint G.S., and Patel S.B. Quantifying raft proteins in neonatal mouse brain by 'tube-gel' protein digestion label-free shotgun proteomics. Proteome Sci 5 (2007) 17
    • (2007) Proteome Sci , vol.5 , pp. 17
    • Yu, H.1    Wakim, B.2    Li, M.3    Halligan, B.4    Tint, G.S.5    Patel, S.B.6
  • 133
    • 33746408762 scopus 로고    scopus 로고
    • The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: II. Evaluation of tandem mass spectrometry methodologies for large-scale protein analysis, and the application of statistical tools for data analysis and interpretation
    • von Haller P.D., Yi E., Donohoe S., Vaughn K., Keller A., Nesvizhskii A.I., et al. The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: II. Evaluation of tandem mass spectrometry methodologies for large-scale protein analysis, and the application of statistical tools for data analysis and interpretation. Mol Cell Proteomics 2 (2003) 428-442
    • (2003) Mol Cell Proteomics , vol.2 , pp. 428-442
    • von Haller, P.D.1    Yi, E.2    Donohoe, S.3    Vaughn, K.4    Keller, A.5    Nesvizhskii, A.I.6
  • 134
    • 33746432742 scopus 로고    scopus 로고
    • The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: I. Statistically annotated datasets for peptide sequences and proteins identified via the application of ICAT and tandem mass spectrometry to proteins copurifying with T cell lipid rafts
    • von Haller P.D., Yi E., Donohoe S., Vaughn K., Keller A., Nesvizhskii A.I., et al. The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: I. Statistically annotated datasets for peptide sequences and proteins identified via the application of ICAT and tandem mass spectrometry to proteins copurifying with T cell lipid rafts. Mol Cell Proteomics 2 (2003) 426-427
    • (2003) Mol Cell Proteomics , vol.2 , pp. 426-427
    • von Haller, P.D.1    Yi, E.2    Donohoe, S.3    Vaughn, K.4    Keller, A.5    Nesvizhskii, A.I.6
  • 135
    • 4444376927 scopus 로고    scopus 로고
    • Proteome analysis of lipid rafts in Jurkat cells characterizes a raft subset that is involved in NF-kappaB activation
    • Tu X., Huang A., Bae D., Slaughter N., Whitelegge J., Crother T., et al. Proteome analysis of lipid rafts in Jurkat cells characterizes a raft subset that is involved in NF-kappaB activation. J Proteome Res 3 (2004) 445-454
    • (2004) J Proteome Res , vol.3 , pp. 445-454
    • Tu, X.1    Huang, A.2    Bae, D.3    Slaughter, N.4    Whitelegge, J.5    Crother, T.6
  • 136
    • 33744494534 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics
    • Gupta N., Wollscheid B., Watts J.D., Scheer B., Aebersold R., and DeFranco A.L. Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics. Nat Immunol 7 (2006) 625-633
    • (2006) Nat Immunol , vol.7 , pp. 625-633
    • Gupta, N.1    Wollscheid, B.2    Watts, J.D.3    Scheer, B.4    Aebersold, R.5    DeFranco, A.L.6
  • 137
    • 29544452310 scopus 로고    scopus 로고
    • A quantitative proteomic analysis of growth factor-induced compositional changes in lipid rafts of human smooth muscle cells
    • MacLellan D.L., Steen H., Adam R.M., Garlick M., Zurakowski D., Gygi S.P., et al. A quantitative proteomic analysis of growth factor-induced compositional changes in lipid rafts of human smooth muscle cells. Proteomics 5 (2005) 4733-4742
    • (2005) Proteomics , vol.5 , pp. 4733-4742
    • MacLellan, D.L.1    Steen, H.2    Adam, R.M.3    Garlick, M.4    Zurakowski, D.5    Gygi, S.P.6


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