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Volumn 9, Issue 3, 2014, Pages

Expressed glycosylphosphatidylinositol-anchored horseradish peroxidase identifies co-clustering molecules in individual lipid raft domains

Author keywords

[No Author keywords available]

Indexed keywords

DECAY ACCELERATING FACTOR; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; HORSERADISH PEROXIDASE; THY 1 ANTIGEN; FREE RADICAL; HYBRID PROTEIN;

EID: 84899800448     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0093054     Document Type: Article
Times cited : (33)

References (45)
  • 1
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K (2010) Lipid rafts as a membrane-organizing principle. Science 327: 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 2
    • 84862800913 scopus 로고    scopus 로고
    • Membrane mechanisms for signal transduction: The coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes
    • Kusumi A, Fujiwara TK, Morone N, Yoshida KJ, Chadda R, et al. (2012) Membrane mechanisms for signal transduction: the coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes. Semin Cell Dev Biol 23: 126-144.
    • (2012) Semin Cell Dev Biol , vol.23 , pp. 126-144
    • Kusumi, A.1    Fujiwara, T.K.2    Morone, N.3    Yoshida, K.J.4    Chadda, R.5
  • 5
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31-39.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 6
    • 0036842936 scopus 로고    scopus 로고
    • Reciprocal raft-receptor interactions and the assembly of adhesion complexes
    • DOI 10.1002/bies.10172
    • Harris TJC, Siu CH (2002) Reciprocal raft-receptor interactions and the assembly of adhesion complexes. Bioessays 24: 996-1003. (Pubitemid 35326157)
    • (2002) BioEssays , vol.24 , Issue.11 , pp. 996-1003
    • Harris, T.J.C.1    Siu, C.-H.2
  • 8
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68: 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 9
    • 34250368055 scopus 로고    scopus 로고
    • Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling
    • DOI 10.1091/mbc.E07-01-0071
    • Fujita A, Cheng J, Hirakawa M, Furukawa K, Kusunoki S, et al. (2007) Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol Biol Cell 18: 2112-2122. (Pubitemid 46911363)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.6 , pp. 2112-2122
    • Fujita, A.1    Cheng, J.2    Hirakawa, M.3    Furakawa, K.4    Kusunoki, S.5    Fujimoto, T.6
  • 10
    • 64749090227 scopus 로고    scopus 로고
    • Segregation of GM1 and GM3 clusters in the cell membrane depends on the intact actin cytoskeleton
    • Fujita A, Cheng J, Fujimoto T (2009) Segregation of GM1 and GM3 clusters in the cell membrane depends on the intact actin cytoskeleton. Biochim Biophys Acta 1791: 388-396.
    • (2009) Biochim Biophys Acta , vol.1791 , pp. 388-396
    • Fujita, A.1    Cheng, J.2    Fujimoto, T.3
  • 11
    • 34248227584 scopus 로고    scopus 로고
    • GPI anchoring of protein in yeast and mammalian cells, or: How we learned to stop worrying and love glycophospholipids
    • DOI 10.1194/jlr.R700002-JLR200
    • Orlean P, Menon AK (2007) Thematic review series: Lipid Posttranslational Modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J Lipid Res 48: 993-1011. (Pubitemid 46708667)
    • (2007) Journal of Lipid Research , vol.48 , Issue.5 , pp. 993-1011
    • Orlean, P.1    Menon, A.K.2
  • 12
    • 0035181218 scopus 로고    scopus 로고
    • Comparative efficiencies of C-terminal signals of native glycophosphatidylinositol (GPI)-anchored proproteins in conferring GPI-anchoring
    • DOI 10.1002/jcb.1267
    • Chen R, Knez JJ, Merrick WC, Medof ME (2002) Comparative efficiencies of C-terminal signals of native glycophosphatidylinositol (GPI)-anchored proproteins in conferring GPI-anchoring. J Cell Biochem 84: 68-83. (Pubitemid 33101512)
    • (2001) Journal of Cellular Biochemistry , vol.84 , Issue.1 , pp. 68-83
    • Chen, R.1    Knez, J.J.2    Merrick, W.C.3    Edward, M.M.4
  • 13
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • DOI 10.1038/29563
    • Varma R, Mayor S (1998) GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394: 798-801. (Pubitemid 28391646)
    • (1998) Nature , vol.394 , Issue.6695 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 15
    • 0032541423 scopus 로고    scopus 로고
    • Cholesterol-dependent retention of GPI-anchored proteins in endosomes
    • DOI 10.1093/emboj/17.16.4626
    • Mayor S, Sabharanjak S, Maxfield FR (1998) Cholesterol-dependent retention of GPI-anchored proteins in endosomes. EMBO J 17: 4626-4638. (Pubitemid 28377163)
    • (1998) EMBO Journal , vol.17 , Issue.16 , pp. 4626-4638
    • Mayor, S.1    Sabharanjak, S.2    Maxfield, F.R.3
  • 16
  • 17
    • 0037031821 scopus 로고    scopus 로고
    • Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein
    • Magalhães AC, Silva JA, Lee KS, Martins VR, Prado VF, et al. (2002) Endocytic intermediates involved with the intracellular trafficking of a fluorescent cellular prion protein. J Biol Chem 277: 33311-33318.
    • (2002) J Biol Chem , vol.277 , pp. 33311-33318
    • Magalhães, A.C.1    Silva, J.A.2    Lee, K.S.3    Martins, V.R.4    Prado, V.F.5
  • 18
    • 11244252192 scopus 로고    scopus 로고
    • Differential insertion of GPI-anchored GFPs into lipid rafts of live cells
    • DOI 10.1096/fj.03-1338fje
    • Legler DF, Doucey MA, Schneider P, Chapatte L, Bender FC, et al. (2004) Differential insertion of GPI-anchored GFPs into lipid rafts of live cells. FASEB J 19: 73-75. (Pubitemid 40069922)
    • (2005) FASEB Journal , vol.19 , Issue.1 , pp. 73-75
    • Legler, D.F.1    Doucey, M.-A.2    Schneider, P.3    Chapatte, L.4    Bender, F.C.5    Bron, C.6
  • 19
    • 84862189303 scopus 로고    scopus 로고
    • GPI-anchor remodeling: Potential functions of GPI-anchors in intracellular trafficking and membrane dynamics
    • Fujita M, Kinoshita T (2012) GPI-anchor remodeling: Potential functions of GPI-anchors in intracellular trafficking and membrane dynamics. Biochim Biophys Acta 1821: 1050-1058.
    • (2012) Biochim Biophys Acta , vol.1821 , pp. 1050-1058
    • Fujita, M.1    Kinoshita, T.2
  • 20
    • 70349838223 scopus 로고    scopus 로고
    • GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi
    • Fujita M, Maeda Y, Ra M, Yamaguchi Y, Taguchi R, et al. (2009) GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi. Cell 139: 352-365.
    • (2009) Cell , vol.139 , pp. 352-365
    • Fujita, M.1    Maeda, Y.2    Ra, M.3    Yamaguchi, Y.4    Taguchi, R.5
  • 21
    • 0032409445 scopus 로고    scopus 로고
    • Sequence properties of GPI-anchored proteins near the omega-site: Constraints for the polypeptide binding site of the putative transamidase
    • Eisenhaber B, Bork P, Eisenhaber F (1998) Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase. Protein Eng 11: 1155-1161. (Pubitemid 29012126)
    • (1998) Protein Engineering , vol.11 , Issue.12 , pp. 1155-1161
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 22
    • 59349120088 scopus 로고    scopus 로고
    • Different GPI-attachment signals affect the oligomerisation of GPI-anchored proteins and their apical sorting
    • Paladino S, Lebreton S, Tivodar S, Campana V, Tempre R, et al. (2008) Different GPI-attachment signals affect the oligomerisation of GPI-anchored proteins and their apical sorting. J Cell Sci 121: 4001-4007.
    • (2008) J Cell Sci , vol.121 , pp. 4001-4007
    • Paladino, S.1    Lebreton, S.2    Tivodar, S.3    Campana, V.4    Tempre, R.5
  • 24
    • 79851486444 scopus 로고    scopus 로고
    • The enzyme-mediated activation of radical source reaction: A new approach to identify partners of a given molecule in membrane microdomains
    • Honke K, Kotani N (2011) The enzyme-mediated activation of radical source reaction: a new approach to identify partners of a given molecule in membrane microdomains. J Neurochem 116: 690-695.
    • (2011) J Neurochem , vol.116 , pp. 690-695
    • Honke, K.1    Kotani, N.2
  • 25
    • 84891610934 scopus 로고    scopus 로고
    • Identification of cell-surface molecular interactions under living conditions by using the enzyme-mediated activation of radical sources (EMARS) method
    • Honke K, Kotani N (2012) Identification of cell-surface molecular interactions under living conditions by using the enzyme-mediated activation of radical sources (EMARS) method. Sensors 12: 16037-16045.
    • (2012) Sensors , vol.12 , pp. 16037-16045
    • Honke, K.1    Kotani, N.2
  • 26
    • 77952746128 scopus 로고    scopus 로고
    • Anomalous expression of Thy1 (CD90) in B-cell lymphoma cells and proliferation inhibition by anti-Thy1 antibody treatment
    • Ishiura Y, Kotani N, Yamashita R, Yamamoto H, Kozutsumi Y, et al. (2010) Anomalous expression of Thy1 (CD90) in B-cell lymphoma cells and proliferation inhibition by anti-Thy1 antibody treatment. Biochem Biophys Res Commun 396: 329-334.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 329-334
    • Ishiura, Y.1    Kotani, N.2    Yamashita, R.3    Yamamoto, H.4    Kozutsumi, Y.5
  • 27
    • 79952285665 scopus 로고    scopus 로고
    • Spatiotemporally-regulated interaction between b1 integrin and ErbB4 that is involved in fibronectin-dependent cell migration
    • Yamashita R, Kotani N, Ishiura Y, Higashiyama S, Honke K (2011) Spatiotemporally-regulated interaction between b1 integrin and ErbB4 that is involved in fibronectin-dependent cell migration. J Biochem 149: 347-355.
    • (2011) J Biochem , vol.149 , pp. 347-355
    • Yamashita, R.1    Kotani, N.2    Ishiura, Y.3    Higashiyama, S.4    Honke, K.5
  • 28
    • 84868234379 scopus 로고    scopus 로고
    • Fibroblast Growth Factor Receptor 3 (FGFR3) associated with the CD20 antigen regulates the rituximab-induced proliferation inhibition in B-cell lymphoma cells
    • Kotani N, Ishiura Y, Yamashita R, Ohnishi T, and Honke K (2012) Fibroblast Growth Factor Receptor 3 (FGFR3) associated with the CD20 antigen regulates the rituximab-induced proliferation inhibition in B-cell lymphoma cells. J Biol Chem 287: 37109-37118.
    • (2012) J Biol Chem , vol.287 , pp. 37109-37118
    • Kotani, N.1    Ishiura, Y.2    Yamashita, R.3    Ohnishi, T.4    Honke, K.5
  • 29
    • 84868099850 scopus 로고    scopus 로고
    • Proteomic analysis of ganglioside-associated membrane molecules: Substantial basis for molecular clustering
    • Hashimoto N, Hamamura K, Kotani N, Furukawa K, Kaneko K, et al. (2012) Proteomic analysis of ganglioside-associated membrane molecules: Substantial basis for molecular clustering. Proteomics 12: 1-10.
    • (2012) Proteomics , vol.12 , pp. 1-10
    • Hashimoto, N.1    Hamamura, K.2    Kotani, N.3    Furukawa, K.4    Kaneko, K.5
  • 30
    • 84855463114 scopus 로고    scopus 로고
    • A proteomics approach to the cell-surface interactome using the enzyme-mediated activation of radical sources reaction
    • Jiang S, Kotani N, Ohnishi T, Miyagawa-Yamguchi A, Tsuda M, et al. (2012) A proteomics approach to the cell-surface interactome using the enzyme-mediated activation of radical sources reaction. Proteomics 12: 54-62.
    • (2012) Proteomics , vol.12 , pp. 54-62
    • Jiang, S.1    Kotani, N.2    Ohnishi, T.3    Miyagawa-Yamguchi, A.4    Tsuda, M.5
  • 31
    • 0242659246 scopus 로고    scopus 로고
    • Vesicular transport route of horseradish C1a peroxidase is regulated by N- and C-terminal propeptides in tobacco cells
    • DOI 10.1007/s00253-003-1273-z
    • Matsui T, Nakayama H, Yoshida K, Shinmyo A (2003) Vesicular transport route of horseradish C1a peroxidase is regulated by N- and C-terminal propeptides in tobacco cells. Appl Microbiol Biotechnol 62: 517-522. (Pubitemid 37372445)
    • (2003) Applied Microbiology and Biotechnology , vol.62 , Issue.5-6 , pp. 517-522
    • Matsui, T.1    Nakayama, H.2    Yoshida, K.3    Shinmyo, A.4
  • 32
    • 0028030082 scopus 로고
    • Mechanisms underlying expression of Tn10 encoded tetracycline resistance
    • Hillen W, Berens C (1994) Mechanisms underlying expression of Tn10 encoded tetracycline resistance. Annu Rev Microbiol 48: 345-369. (Pubitemid 24334101)
    • (1994) Annual Review of Microbiology , vol.48 , pp. 345-369
    • Hillen, W.1    Berens, C.2
  • 33
    • 0032170171 scopus 로고    scopus 로고
    • Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells
    • Yao F, Svensjö T, Winkler T, Lu M, Eriksson C, et al. (1998) Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells. Hum Gene Ther 9: 1939-1950. (Pubitemid 28439099)
    • (1998) Human Gene Therapy , vol.9 , Issue.13 , pp. 1939-1950
    • Yao, F.1    Svensjo, T.2    Winkler, T.3    Lu, M.4    Eriksson, C.5    Eriksson, E.6
  • 34
    • 0022465626 scopus 로고
    • Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PIPLC). Selective modification of a complement regulatory protein
    • DOI 10.1084/jem.163.5.1150
    • Davitz MA, Low MG, Nussenzweig V (1986) Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PIPLC). Selective modification of a complement regulatory protein. J Exp Med 163: 1150-1161. (Pubitemid 16000414)
    • (1986) Journal of Experimental Medicine , vol.163 , Issue.5 , pp. 1150-1161
    • Davitz, M.A.1    Low, M.G.2    Nussenzweig, V.3
  • 35
    • 0027997875 scopus 로고
    • Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase
    • Connolly CN (1994) Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase. J Cell Biol 127: 641-652.
    • (1994) J Cell Biol , vol.127 , pp. 641-652
    • Connolly, C.N.1
  • 36
    • 1942541158 scopus 로고    scopus 로고
    • Glia engulf degenerating axons during developmental axon pruning
    • DOI 10.1016/j.cub.2004.03.035, PII S0960982204002143
    • Watts RJ, Schuldiner O, Perrino J, Larsen C, Luo L (2004) Glia engulf degenerating axons during developmental axon pruning. Curr Biol 14: 678-684. (Pubitemid 38503604)
    • (2004) Current Biology , vol.14 , Issue.8 , pp. 678-684
    • Watts, R.J.1    Schuldiner, O.2    Perrino, J.3    Larsen, C.4    Luo, L.5
  • 37
    • 34547657630 scopus 로고    scopus 로고
    • Horseradish peroxidase cDNA as a marker for electron microscopy in neurons
    • DOI 10.1016/j.jneumeth.2007.06.004, PII S0165027007002749
    • Schikorski T, Young Jr SM, Hu Y (2007) Horseradish peroxidase cDNA as a marker for electron microscopy in neurons. J Neurosci Methods 165: 210-215. (Pubitemid 47212462)
    • (2007) Journal of Neuroscience Methods , vol.165 , Issue.2 , pp. 210-215
    • Schikorski, T.1    Young Jr., S.M.2    Hu, Y.3
  • 38
    • 0017041348 scopus 로고
    • Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)
    • Welinder KG (1976) Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7). FEBS Lett 72: 19-23.
    • (1976) FEBS Lett , vol.72 , pp. 19-23
    • Welinder, K.G.1
  • 39
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • DOI 10.1083/jcb.200407094
    • Paladino S, Sarnataro D, Pillich R, Tivodar S, Nitsch L, et al. (2004) Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J Cell Biol 167: 699-709. (Pubitemid 39565150)
    • (2004) Journal of Cell Biology , vol.167 , Issue.4 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 40
    • 82655189982 scopus 로고    scopus 로고
    • N-Glycosylation instead of cholesterol mediates oligomerization and apical sorting of GPI-APs in FRT cells
    • Imjeti NS, Lebreton S, Paladino S, de la Fuente E, Gonzalez A, et al. (2011) N-Glycosylation instead of cholesterol mediates oligomerization and apical sorting of GPI-APs in FRT cells. Mol Biol Cell 22: 4621-4634.
    • (2011) Mol Biol Cell , vol.22 , pp. 4621-4634
    • Imjeti, N.S.1    Lebreton, S.2    Paladino, S.3    De La Fuente, E.4    Gonzalez, A.5
  • 41
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanova I, Horejsi V, Ansotegui IJ, Knapp W, Stockinger H (1991) GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 254: 1016-1019. (Pubitemid 21917433)
    • (1991) Science , vol.254 , Issue.5034 , pp. 1016-1019
    • Stefanova, I.1    Horejsi, V.2    Ansotegui, I.J.3    Knapp, W.4    Stockinger, H.5
  • 42
    • 0026457327 scopus 로고
    • Signal transduction through decay-accelerating factor. Interaction of glycosyl-phosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn 1
    • Shenoy-Scaria AM, Kwong J, Fujita T, Olszowy MW, Shaw AS, et al. (1992) Signal transduction through decay-accelerating factor. Interaction of glycosyl-phosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn 1. J Immunol 149: 3535-3541.
    • (1992) J Immunol , vol.149 , pp. 3535-3541
    • Shenoy-Scaria, A.M.1    Kwong, J.2    Fujita, T.3    Olszowy, M.W.4    Shaw, A.S.5
  • 43
    • 0027437247 scopus 로고
    • Cross-linking of CD59 and of other glycosyl phosphatidylinositol-anchored molecules on neutrophils triggers cell activation via tyrosine kinase
    • DOI 10.1002/eji.1830231118
    • Morgan BP, van den Berg CW, Davies EV, Hallett MV, Horejsi V (1993) Cross-linking of CD59 and of other glycosyl phosphatidylinositol-anchored molecules on neutrophils triggers cell activation via tyrosine kinase. Eur J Immunol 23: 2841-2850. (Pubitemid 23323558)
    • (1993) European Journal of Immunology , vol.23 , Issue.11 , pp. 2841-2850
    • Morgan, B.P.1    Van Den, B.C.W.2    Davies, E.V.3    Hallett, M.B.4    Horejsi, V.5
  • 45
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and Galpha for temporary cluster immobilization and Lyn activation: Single-molecule tracking study 1
    • DOI 10.1083/jcb.200609174
    • Suzuki KGN, Fujiwara TK, Sanematsu F, Iino R, Edidin M, et al. (2007) GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1. J Cell Biol 177: 717-730. (Pubitemid 46799842)
    • (2007) Journal of Cell Biology , vol.177 , Issue.4 , pp. 717-730
    • Suzuki, K.G.N.1    Fujiwara, T.K.2    Sanematsu, F.3    Iino, R.4    Edidin, M.5    Kusumi, A.6


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