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Volumn 37, Issue 6, 2005, Pages 394-403

Viral entry, lipid rafts and caveosomes

Author keywords

Caveolae; Caveosomes; Echovirus 1; Lipid raft; Simian virus 40; Viral endocytosis

Indexed keywords

CAVEOLA; CAVEOSOME; CELL FUNCTION; CELL ORGANELLE; ECHO VIRUS; ENDOCYTOSIS; HUMAN IMMUNODEFICIENCY VIRUS 1; LIPID RAFT; NONHUMAN; PRIORITY JOURNAL; REVIEW; ROTAVIRUS; SIGNAL TRANSDUCTION; SIMIAN VIRUS 40; VIRUS CELL INTERACTION; VIRUS INFECTION; VIRUS REPLICATION;

EID: 26944489236     PISSN: 07853890     EISSN: 16512219     Source Type: Journal    
DOI: 10.1080/07853890510011976     Document Type: Review
Times cited : (51)

References (114)
  • 1
    • 26944446401 scopus 로고    scopus 로고
    • Viral host cell receptors
    • London: Nature Publishing Group
    • Hyypiä T. Viral host cell receptors. In: Encyclopedia of Life Sciences. London: Nature Publishing Group; 2003.
    • (2003) Encyclopedia of Life Sciences
    • Hyypiä, T.1
  • 4
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • Smith AE, Helenius A. How viruses enter animal cells. Science. 2004;304:237-42.
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 5
    • 0015514472 scopus 로고
    • The fluid-mosaic model of the structure of cell membranes
    • Singer SJ, Nicholson GL. The fluid-mosaic model of the structure of cell membranes. Science. 1972;175:720-31.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicholson, G.L.2
  • 6
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature. 1997;387:569-72.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 7
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton RG. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J Histochem Cytochem. 1994;42:155-66.
    • (1994) J Histochem Cytochem , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 8
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson RG, Jacobson K. A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains. Science. 2002;296:1821-5.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2
  • 9
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 1998;394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 10
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P, Varma R, Sarasij RC, Ira, Gousset K, Krishnamoorthy G, et al. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell. 2004;116:577-89.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira4    Gousset, K.5    Krishnamoorthy, G.6
  • 11
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T, Kurzchalia TV. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature. 1998;394:802-5.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 12
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell. 1992;68:533-44.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 13
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster LJ, De Hoog CL, Mann M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci U S A. 2003; 100:5813-8.
    • (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
  • 14
    • 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, Lisanti MP. Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol. 1993;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
  • 16
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor S, Rothberg KG, Maxfield FR. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science. 1994;264:1948-51.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 17
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol. 2000;1:31-9.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 18
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons K, Ikonen E. How cells handle cholesterol. Science. 2000;290:1721-6.
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 19
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • Schnitzer JE, Oh P, McIntosh DP. Role of GTP hydrolysis in fission of caveolae directly from plasma membranes. Science. 1996;274:239-42.
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 21
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons K, Ehehalt R. Cholesterol, lipid rafts, and disease. J Clin Invest. 2002;110:597-603.
    • (2002) J Clin Invest , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 22
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol. 2003;160:113-23.
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 23
    • 0034158315 scopus 로고    scopus 로고
    • Caveolins and cellular cholesterol balance
    • Ikonen E, Parton RG. Caveolins and cellular cholesterol balance. Traffic. 2000;1:212-7.
    • (2000) Traffic , vol.1 , pp. 212-217
    • Ikonen, E.1    Parton, R.G.2
  • 24
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive? Cell. 2003;115:377-88.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 26
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 2002;296:913-6.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 27
    • 0000855817 scopus 로고
    • Fine structure of blood capillaries
    • Palade G. Fine structure of blood capillaries. J Appl Physiol. 1953;24:1424.
    • (1953) J Appl Physiol , vol.24 , pp. 1424
    • Palade, G.1
  • 28
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epithelium of the mouse
    • Yamada E. The fine structure of the gall bladder epithelium of the mouse. J Biophys Biochem Cytol. 1955;1:455-8.
    • (1955) J Biophys Biochem Cytol , vol.1 , pp. 455-458
    • Yamada, E.1
  • 29
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia TV, Dupree P, Parton RG, Kellner R, Virta H, Lehnert M, et al. VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J Cell Biol. 1992;118:1003-14.
    • (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
  • 30
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae
    • Dietzen DJ, Hastings WR, Lublin DM. Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae. J Biol Chem. 1995;270:6838-42.
    • (1995) J Biol Chem , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 34
    • 0031030664 scopus 로고    scopus 로고
    • Caveolin-3 associates with developing T-tubules during muscle differentiation
    • Parton RG, Way M, Zorzi N, Stang E. Caveolin-3 associates with developing T-tubules during muscle differentiation. J Cell Biol. 1997;136:137-54.
    • (1997) J Cell Biol , vol.136 , pp. 137-154
    • Parton, R.G.1    Way, M.2    Zorzi, N.3    Stang, E.4
  • 35
    • 0030561979 scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • Way M, Parton RG. M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett. 1995;376:108-12.
    • (1995) FEBS Lett , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 36
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart EJ, Ying Y, Donzell WC, Anderson RG. A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J Biol Chem. 1996;271:29427-35.
    • (1996) J Biol Chem , vol.271 , pp. 29427-29435
    • Smart, E.J.1    Ying, Y.2    Donzell, W.C.3    Anderson, R.G.4
  • 37
    • 0031888035 scopus 로고    scopus 로고
    • Regulation of caveolin and caveolae by cholesterol in MDCK cells
    • Hailstones D, Sleer LS, Parton RG, Stanley KK. Regulation of caveolin and caveolae by cholesterol in MDCK cells. J Lipid Res. 1998;39:369-79.
    • (1998) J Lipid Res , vol.39 , pp. 369-379
    • Hailstones, D.1    Sleer, L.S.2    Parton, R.G.3    Stanley, K.K.4
  • 38
    • 0026625261 scopus 로고
    • Lowering the cholesterol content of MA104 cells inhibits receptor-mediated transport of folate
    • Chang WJ, Rothberg KG, Kamen BA, Anderson RG. Lowering the cholesterol content of MA104 cells inhibits receptor-mediated transport of folate. J Cell Biol. 1992;118:63-9.
    • (1992) J Cell Biol , vol.118 , pp. 63-69
    • Chang, W.J.1    Rothberg, K.G.2    Kamen, B.A.3    Anderson, R.G.4
  • 39
    • 0028998554 scopus 로고
    • VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro
    • Monier S, Parton RG, Vogel F, Behlke J, Henske A, Kurzchalia TV. VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro. Mol Biol Cell. 1995;6:911-27.
    • (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
  • 41
    • 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, Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol. 2001;3: 473-83.
    • (2001) Nat Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 42
    • 0033836520 scopus 로고    scopus 로고
    • The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
    • Gagescu R, Demaurex N, Parton RG, Hunziker W, Huber LA, Gruenberg J. The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Mol Biol Cell. 2000;11:2775-91.
    • (2000) Mol Biol Cell , vol.11 , pp. 2775-2791
    • Gagescu, R.1    Demaurex, N.2    Parton, R.G.3    Hunziker, W.4    Huber, L.A.5    Gruenberg, J.6
  • 43
    • 4544375506 scopus 로고    scopus 로고
    • Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
    • Pelkmans L, Burli T, Zerial M, Helenius A. Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic. Cell. 2004;118:767-80.
    • (2004) Cell , vol.118 , pp. 767-780
    • Pelkmans, L.1    Burli, T.2    Zerial, M.3    Helenius, A.4
  • 44
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton RG, Joggerst B, Simons K. Regulated internalization of caveolae. J Cell Biol. 1994;127:1199-215.
    • (1994) J Cell Biol , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 45
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer JE, McIntosh DP, Dvorak AM, Liu J, Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science. 1995;269:1435-9.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 46
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane
    • Mineo C, James GL, Smart EJ, Anderson RG. Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane. J Biol Chem. 1996;271:11930-5.
    • (1996) J Biol Chem , vol.271 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.4
  • 48
    • 0029901663 scopus 로고    scopus 로고
    • Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: Implications for nitric oxide signaling
    • Garcia-Cardena G, Oh P, Liu J, Schnitzer JE, Sessa WC. Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: implications for nitric oxide signaling. Proc Natl Acad Sci U S A. 1996;93:6448-53.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6448-6453
    • Garcia-Cardena, G.1    Oh, P.2    Liu, J.3    Schnitzer, J.E.4    Sessa, W.C.5
  • 49
    • 0024317054 scopus 로고
    • Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus
    • Glenney JR, Jr. Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus. J Biol Chem. 1989;264:20163-6.
    • (1989) J Biol Chem , vol.264 , pp. 20163-20166
    • Glenney Jr., J.R.1
  • 50
  • 51
    • 1342267006 scopus 로고    scopus 로고
    • Caveolinopathies: Mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases
    • Woodman SE, Sotgia F, Galbiati F, Minetti C, Lisanti MP. Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases. Neurology. 2004;62:538-43.
    • (2004) Neurology , vol.62 , pp. 538-543
    • Woodman, S.E.1    Sotgia, F.2    Galbiati, F.3    Minetti, C.4    Lisanti, M.P.5
  • 52
    • 0033178782 scopus 로고    scopus 로고
    • Caveolin-3 upregulation activates beta-secretase-mediated cleavage of the amyloid precursor protein in Alzheimer's disease
    • Nishiyama K, Trapp BD, Ikezu T, Ransohoff RM, Tomita T, Iwatsubo T, et al. Caveolin-3 upregulation activates beta-secretase-mediated cleavage of the amyloid precursor protein in Alzheimer's disease. J Neurosci. 1999;19:6538-48.
    • (1999) J Neurosci , vol.19 , pp. 6538-6548
    • Nishiyama, K.1    Trapp, B.D.2    Ikezu, T.3    Ransohoff, R.M.4    Tomita, T.5    Iwatsubo, T.6
  • 53
    • 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. 2001;293:2449-52.
    • (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
  • 55
    • 0037113074 scopus 로고    scopus 로고
    • Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton
    • Mundy DI, Machleidt T, Ying YS, Anderson RG, Bloom GS. Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton. J Cell Sci. 2002;115:4327-39.
    • (2002) J Cell Sci , vol.115 , pp. 4327-4339
    • Mundy, D.I.1    Machleidt, T.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5
  • 57
    • 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, McIntosh DP, Schnitzer JE. 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. 1998;141:101-14.
    • (1998) J Cell Biol , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 58
    • 0027952583 scopus 로고
    • Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae
    • Smart EJ, Foster DC, Ying YS, Kamen BA, Anderson RG. Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae. J Cell Biol. 1994;124:307-13.
    • (1994) J Cell Biol , vol.124 , pp. 307-313
    • Smart, E.J.1    Foster, D.C.2    Ying, Y.S.3    Kamen, B.A.4    Anderson, R.G.5
  • 59
    • 0029560256 scopus 로고
    • Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps
    • Conrad PA, Smart EJ, Ying YS, Anderson RG, Bloom GS. Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps. J Cell Biol. 1995;131:1421-33.
    • (1995) J Cell Biol , vol.131 , pp. 1421-1433
    • Conrad, P.A.1    Smart, E.J.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5
  • 60
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke H, Baba T, Warnock DE, Schmid SL. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J Cell Biol. 1994;127:915-34.
    • (1994) J Cell Biol , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 61
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway
    • Lamaze C, Dujeancourt A, Baba T, Lo CG, Benmerah A, Dautry-Varsat A. Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol Cell. 2001;7:661-71.
    • (2001) Mol Cell , vol.7 , pp. 661-671
    • Lamaze, C.1    Dujeancourt, A.2    Baba, T.3    Lo, C.G.4    Benmerah, A.5    Dautry-Varsat, A.6
  • 63
    • 0031847686 scopus 로고    scopus 로고
    • Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum
    • Benlimame N, Le PU, Nabi IR. Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum. Mol Biol Cell. 1998;9:1773-86.
    • (1998) Mol Biol Cell , vol.9 , pp. 1773-1786
    • Benlimame, N.1    Le, P.U.2    Nabi, I.R.3
  • 64
    • 0019994630 scopus 로고
    • Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins
    • Montesano R, Roth J, Robert A, Orci L. Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins. Nature. 1982;296:651-3.
    • (1982) Nature , vol.296 , pp. 651-653
    • Montesano, R.1    Roth, J.2    Robert, A.3    Orci, L.4
  • 65
    • 0036094927 scopus 로고    scopus 로고
    • A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex
    • Nichols BJ. A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex. Nat Cell Biol. 2002;4:374-8.
    • (2002) Nat Cell Biol , vol.4 , pp. 374-378
    • Nichols, B.J.1
  • 66
    • 0034604515 scopus 로고    scopus 로고
    • Involvement of cellular caveolae in bacterial entry into mast cells
    • Shin JS, Gao Z, Abraham SN. Involvement of cellular caveolae in bacterial entry into mast cells. Science. 2000;289:785-8.
    • (2000) Science , vol.289 , pp. 785-788
    • Shin, J.S.1    Gao, Z.2    Abraham, S.N.3
  • 67
    • 0036239115 scopus 로고    scopus 로고
    • Endocytosis via caveolae
    • Pelkmans L, Helenius A. Endocytosis via caveolae. Traffic. 2002;3:311-20.
    • (2002) Traffic , vol.3 , pp. 311-320
    • Pelkmans, L.1    Helenius, A.2
  • 69
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • Damm EM, Pelkmans L, Kartenbeck J, Mezzacasa A, Kurzchalia T, Helenius A. Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J Cell Biol. 2005;168: 477-88.
    • (2005) J Cell Biol , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzchalia, T.5    Helenius, A.6
  • 70
    • 0037444495 scopus 로고    scopus 로고
    • Distinct caveolae-mediated endocytic pathways target the Golgi apparatus and the endoplasmic reticulum
    • Le PU, Nabi IR. Distinct caveolae-mediated endocytic pathways target the Golgi apparatus and the endoplasmic reticulum. J Cell Sci. 2003;116:1059-71.
    • (2003) J Cell Sci , vol.116 , pp. 1059-1071
    • Le, P.U.1    Nabi, I.R.2
  • 71
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson HA, Chen Y, Norkin LC. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol Biol Cell. 1996;7:1825-34.
    • (1996) Mol Biol Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 72
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L, Puntener D, Helenius A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science. 2002;296: 535-9.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 74
    • 6344275643 scopus 로고    scopus 로고
    • Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events
    • Pietiäinen V, Marjomäki V, Upla P, Pelkmans L, Helenius A, Hyypiä T. Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events. Mol Biol Cell. 2004;15:4911-25.
    • (2004) Mol Biol Cell , vol.15 , pp. 4911-4925
    • Pietiäinen, V.1    Marjomäki, V.2    Upla, P.3    Pelkmans, L.4    Helenius, A.5    Hyypiä, T.6
  • 75
    • 0034755553 scopus 로고    scopus 로고
    • Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei
    • Richterova Z, Liebl D, Horak M, Palkova Z, Stokrova J, Hozak P, et al. Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei. J Virol. 2001;75:10880-91.
    • (2001) J Virol , vol.75 , pp. 10880-10891
    • Richterova, Z.1    Liebl, D.2    Horak, M.3    Palkova, Z.4    Stokrova, J.5    Hozak, P.6
  • 77
    • 3543131798 scopus 로고    scopus 로고
    • Human coronavirus 229E binds to CD13 in rafts and enters the cell through caveolae
    • Nomura R, Kiyota A, Suzaki E, Kataoka K, Ohe Y, Miyamoto K, et al. Human coronavirus 229E binds to CD13 in rafts and enters the cell through caveolae. J Virol. 2004;78:8701-8.
    • (2004) J Virol , vol.78 , pp. 8701-8708
    • Nomura, R.1    Kiyota, A.2    Suzaki, E.3    Kataoka, K.4    Ohe, Y.5    Miyamoto, K.6
  • 78
    • 0037334521 scopus 로고    scopus 로고
    • Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells
    • Bousarghin L, Touze A, Sizaret PY, Coursaget P. Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells. J Virol. 2003;77:3846-50.
    • (2003) J Virol , vol.77 , pp. 3846-3850
    • Bousarghin, L.1    Touze, A.2    Sizaret, P.Y.3    Coursaget, P.4
  • 79
    • 4444370896 scopus 로고    scopus 로고
    • Analysis of the interaction between respiratory syncytial virus and lipid-rafts in Hep2 cells during infection
    • Brown G, Jeffree CE, McDonald T, Rixon HW, Aitken JD, Sugrue RJ. Analysis of the interaction between respiratory syncytial virus and lipid-rafts in Hep2 cells during infection. Virology. 2004;327:175-85.
    • (2004) Virology , vol.327 , pp. 175-185
    • Brown, G.1    Jeffree, C.E.2    McDonald, T.3    Rixon, H.W.4    Aitken, J.D.5    Sugrue, R.J.6
  • 80
    • 0033034166 scopus 로고    scopus 로고
    • Involvement of caveolae in the uptake of respiratory syncytial virus antigen by dendritic cells
    • Werling D, Hope JC, Chaplin P, Collins RA, Taylor G, Howard CJ. Involvement of caveolae in the uptake of respiratory syncytial virus antigen by dendritic cells. J Leukoc Biol. 1999;66:50-8.
    • (1999) J Leukoc Biol , vol.66 , pp. 50-58
    • Werling, D.1    Hope, J.C.2    Chaplin, P.3    Collins, R.A.4    Taylor, G.5    Howard, C.J.6
  • 82
    • 8744221758 scopus 로고    scopus 로고
    • Characterization of simian virus 40 on its infectious entry pathway in cells using fluorescence correlation spectroscopy
    • Bernacchi S, Mueller G, Langowski J, Waldeck W. Characterization of simian virus 40 on its infectious entry pathway in cells using fluorescence correlation spectroscopy. Biochem Soc Trans. 2004;32:746-9.
    • (2004) Biochem Soc Trans , vol.32 , pp. 746-749
    • Bernacchi, S.1    Mueller, G.2    Langowski, J.3    Waldeck, W.4
  • 83
    • 0031861436 scopus 로고    scopus 로고
    • MHC class I molecules are enriched in caveolae but do not enter with simian virus 40
    • Anderson HA, Chen Y, Norkin LC. MHC class I molecules are enriched in caveolae but do not enter with simian virus 40. J Gen Virol. 1998;79:1469-77.
    • (1998) J Gen Virol , vol.79 , pp. 1469-1477
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 84
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolae
    • Stang E, Kartenbeck J, Parton RG. Major histocompatibility complex class I molecules mediate association of SV40 with caveolae. Mol Biol Cell. 1997;8:47-57.
    • (1997) Mol Biol Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 85
    • 0041765800 scopus 로고    scopus 로고
    • Insider information: What viruses tell us about endocytosis
    • Pelkmans L, Helenius A. Insider information: what viruses tell us about endocytosis. Curr Opin Cell Biol. 2003;15:414-22.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 414-422
    • Pelkmans, L.1    Helenius, A.2
  • 86
    • 0029818007 scopus 로고    scopus 로고
    • Extracellular simian virus 40 induces an ERK/MAP kinase-independent signalling pathway that activates primary response genes and promotes virus entry
    • Dangoria NS, Breau WC, Anderson HA, Cishek DM, Norkin LC. Extracellular simian virus 40 induces an ERK/MAP kinase-independent signalling pathway that activates primary response genes and promotes virus entry. J Gen Virol. 1996;77:2173-82.
    • (1996) J Gen Virol , vol.77 , pp. 2173-2182
    • Dangoria, N.S.1    Breau, W.C.2    Anderson, H.A.3    Cishek, D.M.4    Norkin, L.C.5
  • 87
    • 0033145517 scopus 로고    scopus 로고
    • Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains
    • Roy S, Luetterforst R, Harding A, Apolloni A, Etheridge M, Stang E, et al. Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains. Nat Cell Biol. 1999;1:98-105.
    • (1999) Nat Cell Biol , vol.1 , pp. 98-105
    • Roy, S.1    Luetterforst, R.2    Harding, A.3    Apolloni, A.4    Etheridge, M.5    Stang, E.6
  • 88
    • 0036000023 scopus 로고    scopus 로고
    • Inhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection
    • Richards AA, Stang E, Pepperkok R, Parton RG. Inhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection. Mol Biol Cell. 2002;13:1750-64.
    • (2002) Mol Biol Cell , vol.13 , pp. 1750-1764
    • Richards, A.A.1    Stang, E.2    Pepperkok, R.3    Parton, R.G.4
  • 89
    • 0031785929 scopus 로고    scopus 로고
    • How do animal DNA viruses get to the nucleus?
    • Kasamatsu H, Nakanishi A. How do animal DNA viruses get to the nucleus? Annu Rev Microbiol. 1998;52:627-86.
    • (1998) Annu Rev Microbiol , vol.52 , pp. 627-686
    • Kasamatsu, H.1    Nakanishi, A.2
  • 90
    • 0344872570 scopus 로고    scopus 로고
    • Ganglioside-dependent cell attachment and endocytosis of murine polyomavirus-like particles
    • Smith AE, Lilie H, Helenius A. Ganglioside-dependent cell attachment and endocytosis of murine polyomavirus-like particles. FEBS Lett. 2003;555:199-203.
    • (2003) FEBS Lett , vol.555 , pp. 199-203
    • Smith, A.E.1    Lilie, H.2    Helenius, A.3
  • 91
    • 0037321752 scopus 로고    scopus 로고
    • Cell penetration and trafficking of polyomavirus
    • Gilbert JM, Goldberg IG, Benjamin TL. Cell penetration and trafficking of polyomavirus. J Virol. 2003;77:2615-22.
    • (2003) J Virol , vol.77 , pp. 2615-2622
    • Gilbert, J.M.1    Goldberg, I.G.2    Benjamin, T.L.3
  • 92
    • 0033851301 scopus 로고    scopus 로고
    • Early steps of polyomavirus entry into cells
    • Gilbert JM, Benjamin TL. Early steps of polyomavirus entry into cells. J Virol. 2000;74:8582-8.
    • (2000) J Virol , vol.74 , pp. 8582-8588
    • Gilbert, J.M.1    Benjamin, T.L.2
  • 93
    • 7744246474 scopus 로고    scopus 로고
    • Uptake pathway of polyomavirus via ganglioside GD1a
    • Gilbert J, Benjamin T. Uptake pathway of polyomavirus via ganglioside GD1a. J Virol. 2004;78:12259-67.
    • (2004) J Virol , vol.78 , pp. 12259-12267
    • Gilbert, J.1    Benjamin, T.2
  • 96
  • 97
    • 12144290479 scopus 로고    scopus 로고
    • Structural and functional analysis of integrin alpha2I domain interaction with echovirus 1
    • Xing L, Huhtala M, Pietiäinen V, Käpyla J, Vuorinen K, Marjomäki V, et al. Structural and functional analysis of integrin alpha2I domain interaction with echovirus 1. J Biol Chem. 2004;279:11632-8.
    • (2004) J Biol Chem , vol.279 , pp. 11632-11638
    • Xing, L.1    Huhtala, M.2    Pietiäinen, V.3    Käpyla, J.4    Vuorinen, K.5    Marjomäki, V.6
  • 98
    • 0742305342 scopus 로고    scopus 로고
    • Clustering induces a lateral redistribution of alpha 2 beta 1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization
    • Upla P, Marjomäki V, Kankaanpää P, Ivaska J, Hyypiä T, Van Der Goot FG, et al. Clustering induces a lateral redistribution of alpha 2 beta 1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization. Mol Biol Cell. 2004;15:625-36.
    • (2004) Mol Biol Cell , vol.15 , pp. 625-636
    • Upla, P.1    Marjomäki, V.2    Kankaanpää, P.3    Ivaska, J.4    Hyypiä, T.5    Van Der Goot, F.G.6
  • 99
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
    • Pelkmans L, Fava E, Grabner H, Hannus M, Habermann B, Krausz E, et al. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature. 2005.
    • (2005) Nature
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3    Hannus, M.4    Habermann, B.5    Krausz, E.6
  • 100
    • 0037303326 scopus 로고    scopus 로고
    • Two retroviral entry pathways distinguished by lipid raft association of the viral receptor and differences in viral infectivity
    • Narayan S, Barnard RJ, Young JA. Two retroviral entry pathways distinguished by lipid raft association of the viral receptor and differences in viral infectivity. J Virol. 2003;77:1977-83.
    • (2003) J Virol , vol.77 , pp. 1977-1983
    • Narayan, S.1    Barnard, R.J.2    Young, J.A.3
  • 102
    • 4143074753 scopus 로고    scopus 로고
    • Measles virus interacts with and alters signal transduction in T-cell lipid rafts
    • Avota E, Muller N, Klett M, Schneider-Schaulies S. Measles virus interacts with and alters signal transduction in T-cell lipid rafts. J Virol. 2004;78:9552-9.
    • (2004) J Virol , vol.78 , pp. 9552-9559
    • Avota, E.1    Muller, N.2    Klett, M.3    Schneider-Schaulies, S.4
  • 103
    • 0036721021 scopus 로고    scopus 로고
    • A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts
    • Stuart AD, Eustace HE, McKee TA, Brown TD. A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts. J Virol. 2002;76:9307-22.
    • (2002) J Virol , vol.76 , pp. 9307-9322
    • Stuart, A.D.1    Eustace, H.E.2    McKee, T.A.3    Brown, T.D.4
  • 104
    • 0346367067 scopus 로고    scopus 로고
    • Lipid raft microdomains: Key sites for Coxsackievirus A9 infectious cycle
    • Triantafilou K, Triantafilou M. Lipid raft microdomains: key sites for Coxsackievirus A9 infectious cycle. Virology. 2003;317:128-35.
    • (2003) Virology , vol.317 , pp. 128-135
    • Triantafilou, K.1    Triantafilou, M.2
  • 105
    • 3242662811 scopus 로고    scopus 로고
    • Lipid-raft-dependent Coxsackievirus B4 internalization and rapid targeting to the Golgi
    • Triantafilou K, Triantafilou M. Lipid-raft-dependent Coxsackievirus B4 internalization and rapid targeting to the Golgi. Virology. 2004;326:6-19.
    • (2004) Virology , vol.326 , pp. 6-19
    • Triantafilou, K.1    Triantafilou, M.2
  • 107
    • 0028054305 scopus 로고
    • Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method
    • Ward T, Pipkin PA, Clarkson NA, Stone DM, Minor PD, Almond JW. Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method. EMBO J. 1994; 13:5070-4.
    • (1994) EMBO J , vol.13 , pp. 5070-5074
    • Ward, T.1    Pipkin, P.A.2    Clarkson, N.A.3    Stone, D.M.4    Minor, P.D.5    Almond, J.W.6
  • 108
    • 1942489100 scopus 로고    scopus 로고
    • Rotavirus RRV associates with lipid membrane microdomains during cell entry
    • Isa P, Realpe M, Romero P, Lopez S, Arias CF. Rotavirus RRV associates with lipid membrane microdomains during cell entry. Virology. 2004;322:370-81.
    • (2004) Virology , vol.322 , pp. 370-381
    • Isa, P.1    Realpe, M.2    Romero, P.3    Lopez, S.4    Arias, C.F.5
  • 109
    • 0036354940 scopus 로고    scopus 로고
    • Anchorage of HIV on permissive cells leads to coaggregation of viral particles with surface nucleolin at membrane raft microdomains
    • Nisole S, Krust B, Hovanessian AG. Anchorage of HIV on permissive cells leads to coaggregation of viral particles with surface nucleolin at membrane raft microdomains. Exp Cell Res. 2002;276:155-73.
    • (2002) Exp Cell Res , vol.276 , pp. 155-173
    • Nisole, S.1    Krust, B.2    Hovanessian, A.G.3
  • 110
    • 0036239931 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 uses lipid raft-colocalized CD4 and chemokine receptors for productive entry into CD4(+) T cells
    • Popik W, Alee TM, Au WC. Human immunodeficiency virus type 1 uses lipid raft-colocalized CD4 and chemokine receptors for productive entry into CD4(+) T cells. J Virol. 2002;76:4709-22.
    • (2002) J Virol , vol.76 , pp. 4709-4722
    • Popik, W.1    Alee, T.M.2    Au, W.C.3
  • 112
    • 0036284366 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 enters brain microvascular endothelia by macropinocytosis dependent on lipid rafts and the mitogen-activated protein kinase signaling pathway
    • Liu NQ, Lossinsky AS, Popik W, Li X, Gujuluva C, Kriederman B, et al. Human immunodeficiency virus type 1 enters brain microvascular endothelia by macropinocytosis dependent on lipid rafts and the mitogen-activated protein kinase signaling pathway. J Virol. 2002;76:6689-700.
    • (2002) J Virol , vol.76 , pp. 6689-6700
    • Liu, N.Q.1    Lossinsky, A.S.2    Popik, W.3    Li, X.4    Gujuluva, C.5    Kriederman, B.6
  • 113
    • 0037474303 scopus 로고    scopus 로고
    • HIV-1 entry into T-cells is not dependent on CD4 and CCR5 localization to sphingolipid-enriched, detergent-resistant, raft membrane domains
    • Percherancier Y, Lagane B, Planchenault T, Staropoli I, Altmeyer R, Virelizier JL, et al. HIV-1 entry into T-cells is not dependent on CD4 and CCR5 localization to sphingolipid-enriched, detergent-resistant, raft membrane domains. J Biol Chem. 2003;278:3153-61.
    • (2003) J Biol Chem , vol.278 , pp. 3153-3161
    • Percherancier, Y.1    Lagane, B.2    Planchenault, T.3    Staropoli, I.4    Altmeyer, R.5    Virelizier, J.L.6
  • 114
    • 0347052860 scopus 로고    scopus 로고
    • CD4 receptor localized to non-raft membrane microdomains supports HIV-1 entry. Identification of a novel raft localization marker in CD4
    • Popik W, Alee TM. CD4 receptor localized to non-raft membrane microdomains supports HIV-1 entry. Identification of a novel raft localization marker in CD4. J Biol Chem. 2004;279:704-12.
    • (2004) J Biol Chem , vol.279 , pp. 704-712
    • Popik, W.1    Alee, T.M.2


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