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Volumn 9, Issue 4, 1997, Pages 534-542

Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains

Author keywords

[No Author keywords available]

Indexed keywords

ANNEXIN; CAVEOLIN; CHOLESTEROL; GLYCOSPHINGOLIPID; MEMBRANE LIPID; SPHINGOLIPID;

EID: 0030878573     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80030-0     Document Type: Article
Times cited : (724)

References (75)
  • 1
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E: Functional rafts in cell membranes. Nature 1997, 387:569-572. This article for the first time puts forward the concept that sphingolipid-choleslerol rafts are generally used as platforms for membrane-linked functions. It proposes how rafts are formed and how they exert their function by concentrating specific proteins that are raft-associated while excluding others.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 2
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen E, Tagaya M, Ullrich O, Montecucco C, Simons K: Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell 1995, 81:571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 3
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K, van Meer G: Lipid sorting in epithelial cells. Biochemistry 1988, 27:6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 5
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G-protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • •] show that apical and basolateral cognate routes from the TGN to the plasma membane exist in fibroblasts. These findings indicate that rafts are involved in membrane traffic of multiple cell types and are not restricted to overtly polarized cells.
    • (1996) J Cell Biol , vol.133 , pp. 543-558
    • Müsch, A.1    Xu, H.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 6
    • 0029994378 scopus 로고    scopus 로고
    • Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases
    • Deckert M, Ticchioni M, Bernard A: Endocytosis of GPI-anchored proteins in human lymphocytes: role of glycolipid-based domains, actin cytoskeleton, and protein kinases. J Cell Biol 1996, 133:791-799. This paper shows that clustered GPI-anchored proteins are endocytosed in lymphocytes probably via a clathrin-independent mechanism. As lymphocytes do not express caveolin, endocytosis of raft domains with clustered GPI-anchored proteins does not depend on caveolae, which have also been shown to be a vehicle for internalization in [7].
    • (1996) J Cell Biol , vol.133 , pp. 791-799
    • Deckert, M.1    Ticchioni, M.2    Bernard, A.3
  • 7
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton RG, Joggerst B, Simons K: Regulated internalization of caveolae. J Cell Biol 1994, 127:1199-1215.
    • (1994) J Cell Biol , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 8
    • 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, 274:239-242.
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 9
    • 0027415690 scopus 로고
    • Potocytosis of small molecules and ions by caveolae
    • Anderson RGW: Potocytosis of small molecules and ions by caveolae. Trends Cell Biol 1993, 3:69-72.
    • (1993) Trends Cell Biol , vol.3 , pp. 69-72
    • Anderson, R.G.W.1
  • 10
    • 0027269661 scopus 로고
    • The tyrosine kinase connection: How GPI-anchored proteins activate T cells
    • Brown D: The tyrosine kinase connection: how GPI-anchored proteins activate T cells. Curr Opin Immunol 1993, 5:349-354.
    • (1993) Curr Opin Immunol , vol.5 , pp. 349-354
    • Brown, D.1
  • 12
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • Boggs JM: Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function. Biochim Biophys Acta 1987, 906:353-404.
    • (1987) Biochim Biophys Acta , vol.906 , pp. 353-404
    • Boggs, J.M.1
  • 13
    • 0019336197 scopus 로고
    • Sphingomyelins in bilayers and biological membranes
    • Barenholz Y, Thompson TE: Sphingomyelins in bilayers and biological membranes. Biochim Biophys Acta 1980, 604:129-158.
    • (1980) Biochim Biophys Acta , vol.604 , pp. 129-158
    • Barenholz, Y.1    Thompson, T.E.2
  • 14
    • 0029945751 scopus 로고    scopus 로고
    • Cholesterol-induced interfacial area condensation of galactosylceramides and sphingomyelins with identical acyl chains
    • Smaby JM, Momsen M, Kulkarni VS, Brown RE: Cholesterol-induced interfacial area condensation of galactosylceramides and sphingomyelins with identical acyl chains. Biochemistry 1996, 35:5696-5704.
    • (1996) Biochemistry , vol.35 , pp. 5696-5704
    • Smaby, J.M.1    Momsen, M.2    Kulkarni, V.S.3    Brown, R.E.4
  • 15
    • 0028034850 scopus 로고
    • Interaction of cholesterol with sphingomyelin in monolayers and vesicles
    • Bittman R, Kasireddy CR, Mattjus P, Slotte JP: Interaction of cholesterol with sphingomyelin in monolayers and vesicles. Biochemistry 1994, 33:1 1776-11781.
    • (1994) Biochemistry , vol.33 , pp. 11776-11781
    • Bittman, R.1    Kasireddy, C.R.2    Mattjus, P.3    Slotte, J.P.4
  • 16
    • 0027180191 scopus 로고
    • Phase topology and percolation in multiphase bilayers: Is the biological membrane a domain mosaic?
    • Vaz WL, Almeida PF: Phase topology and percolation in multiphase bilayers: is the biological membrane a domain mosaic? Curr Opin Cell Boil 1993, 3:482-488.
    • (1993) Curr Opin Cell Boil , vol.3 , pp. 482-488
    • Vaz, W.L.1    Almeida, P.F.2
  • 17
    • 0028131711 scopus 로고
    • Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers
    • Chong PL: Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers. Proc Natl Acad Sci USA 1994, 91:10069-10073.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10069-10073
    • Chong, P.L.1
  • 18
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher MS, Munro S: Cholesterol and the Golgi apparatus. Science 1993, 261:1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 19
    • 79959449100 scopus 로고
    • Plasma membrane phospholipid asymmetry and its maintenance: The human erythrocyte as a model
    • Edited by Hoekstra D. San Diego: Academic Press
    • Roelofsen B, Op den Kamp JAF: Plasma membrane phospholipid asymmetry and its maintenance: the human erythrocyte as a model. In Cell Lipids. Edited by Hoekstra D. San Diego: Academic Press; 1994:7-46.
    • (1994) Cell Lipids , pp. 7-46
    • Roelofsen, B.1    Op Den Kamp, J.A.F.2
  • 20
    • 0028837910 scopus 로고
    • Glycosphingolipid fatty acid arrangement in phospholipid bilayers: Cholesterol effects
    • Morrow MR, Singh D, Lu D, Grant CWM: Glycosphingolipid fatty acid arrangement in phospholipid bilayers: cholesterol effects. Biophys J 1995, 68:179-186.
    • (1995) Biophys J , vol.68 , pp. 179-186
    • Morrow, M.R.1    Singh, D.2    Lu, D.3    Grant, C.W.M.4
  • 21
    • 0028009878 scopus 로고
    • Do the long fatty acids of the sphingolipids interdigitate across the center of the bilayer of shorter chain symmetric phospholipids?
    • Boggs JM, Koshy KM: Do the long fatty acids of the sphingolipids interdigitate across the center of the bilayer of shorter chain symmetric phospholipids? Biochim Biophys Acta 1994, 1189:233-241.
    • (1994) Biochim Biophys Acta , vol.1189 , pp. 233-241
    • Boggs, J.M.1    Koshy, K.M.2
  • 22
    • 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, 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 23
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton RG, Simons K: Digging into caveolae. Science 1995, 269:1398-1399.
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 24
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance to lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder R, London E, Brown D: Interactions between saturated acyl chains confer detergent resistance to lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc Natl Acad Sci USA 1994, 91:12130-12134.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 25
    • 0028955507 scopus 로고
    • Involvement of detergent-insoluble complexes in the intracellular transport of intestinal brush border enzymes
    • Danielsen EM: Involvement of detergent-insoluble complexes in the intracellular transport of intestinal brush border enzymes. Biochemistry 1995, 34:1596-1605.
    • (1995) Biochemistry , vol.34 , pp. 1596-1605
    • Danielsen, E.M.1
  • 26
    • 0024547523 scopus 로고
    • Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens JE, Roth MG, Matlin KS: Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J Cell Biol 1989, 108:821-832.
    • (1989) J Cell Biol , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 27
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu A, Avalos RT, Sanderson CM, Nayak DP: Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J Virol 1996, 70:6508-6515. Swapping the transmembrane domains of the influenza virus neuraminidase (NA) and the transferrin receptor shows that the NA transmembrane domain contains features conferring apical sorting. This possibly reflects a specific interaction of NA with raft domains which are platforms for apical sorting.
    • (1996) J Virol , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 28
    • 0026667338 scopus 로고
    • Interactions between GPI-anchored proteins and membrane lipids
    • Brown DA: Interactions between GPI-anchored proteins and membrane lipids. Trends Cell Biol 1992, 2:338-343.
    • (1992) Trends Cell Biol , vol.2 , pp. 338-343
    • Brown, D.A.1
  • 29
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville MJ, Ferguson MAJ: The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem J 1993, 294:305-324.
    • (1993) Biochem J , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.J.2
  • 30
    • 0028947029 scopus 로고
    • Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes
    • Hanada K, Nishijima M, Akamatsu Y, Pagano RE: Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes. J Biol Chem 1995, 270:6254-6260.
    • (1995) J Biol Chem , vol.270 , pp. 6254-6260
    • Hanada, K.1    Nishijima, M.2    Akamatsu, Y.3    Pagano, R.E.4
  • 31
    • 0027468760 scopus 로고
    • Detergent insolubility of alkaline phophatase during biosynthetic transport and endocytosis. Role of cholesterol
    • Cerneus DP, Ueffing E, Posthuma G, Strous GJ, van der Ende A: Detergent insolubility of alkaline phophatase during biosynthetic transport and endocytosis. Role of cholesterol. J Biol Chem 1993, 268:3150-3155.
    • (1993) J Biol Chem , vol.268 , pp. 3150-3155
    • Cerneus, D.P.1    Ueffing, E.2    Posthuma, G.3    Strous, G.J.4    Van Der Ende, A.5
  • 32
    • 0028175989 scopus 로고
    • Cysteine(3) of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae
    • Shenoy-Scaria AM, Dietzen DJ, Kwong J, Link DC, Lublin DM: Cysteine(3) of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae. J Cell Biol 1994, 126:353-363.
    • (1994) J Cell Biol , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 33
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl-phosphatidyl-anchored protein targeting to a glycolipid-enriched membrane fraction
    • Rodgers W, Crise B, Rose JK: Signals determining protein tyrosine kinase and glycosyl-phosphatidyl-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol Cell Biol 1994, 14:5384-5391.
    • (1994) Mol Cell Biol , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 34
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-kinases govern their attachment to membranes and association with caveolae
    • Robbins SM, Quintrell NA, Bishop JM: Myristoylation and differential palmitoylation of the HCK protein-kinases govern their attachment to membranes and association with caveolae. Mol Cell Biol 1995, 15:3507-3515.
    • (1995) Mol Cell Biol , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 35
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan G, Parenti M, Magee Al: The dynamic role of palmitoylation in signal transduction. Trends Biochem Sci 1995, 20:181-186.
    • (1995) Trends Biochem Sci , vol.20 , pp. 181-186
    • Milligan, G.1    Parenti, M.2    Magee, Al.3
  • 36
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby SM: Reversible palmitoylation of signaling proteins. Curr Opin Cell Biol 1997, 9:148-154. This review and the previous article [35] put forward the interesting possibility that reversible palmitoylation could constitute a mechanism for regulation of signalling molecules by modifying their association with raft microdomains.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 37
    • 84866476582 scopus 로고    scopus 로고
    • 2-terminal myristoylation and palmitoylation at cysteine-3
    • tyn is rapidly anchored into cell membranes after its biosynthesis. As shown by detailed mutational analysis, this anchoring requires double acylation in the amino-terminal region of the molecule. DIG association of the PTK occurs with a time lag of 10-20 minutes after membrane association, showing sequential membrane binding and partitioning into TX100-insoluble membrane domains.
    • (1997) J Cell Biol , vol.136 , pp. 1023-1035
    • Van't Hof, W.1    Resh, M.D.2
  • 40
    • 0027275642 scopus 로고
    • Signal transducing molecules and GPI-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z, Lisanti MP: Signal transducing molecules and GPI-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
  • 41
    • 0028060685 scopus 로고
    • 2 complex is the major protein component of the Triton X-100-insoluble low-density fraction prepared from MDCK cells in the presence of Ca2+
    • 2 complex is the major protein component of the Triton X-100-insoluble low-density fraction prepared from MDCK cells in the presence of Ca2+. Biochem Biophys Acta 1994, 1223:375-382.
    • (1994) Biochem Biophys Acta , vol.1223 , pp. 375-382
    • Harder, T.1    Gerke, V.2
  • 42
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol
    • Harder T, Kellner R, Parton RG, Gruenberg J: Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. Mol Biol Cell 1997, 8:533-545. Annexin II - tightly bound to cellular membranes - is released, together with a specific set of cortical cytoskeletal proteins, upon pertubation of membrane cholesterol with filipin and digitonin. These cortical cytoskeletal proteins can be immunoprecipitated as a complex with annexin II. These data place annexin II into the interface between the cholesterol-rich membrane domains and the cortical actin cytoskeleton.
    • (1997) Mol Biol Cell , vol.8 , pp. 533-545
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 44
    • 0028921025 scopus 로고
    • Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane
    • Fiedler K, Lafont F, Parton RG, Simons K: Annexin XIIIb: a novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane. J Cell Biol 1995, 128:1043-1053.
    • (1995) J Cell Biol , vol.128 , pp. 1043-1053
    • Fiedler, K.1    Lafont, F.2    Parton, R.G.3    Simons, K.4
  • 45
    • 0026575153 scopus 로고
    • A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: Characterization of a novel gut-specific N-myristoylated annexin
    • Wice BM, Gordon JI: A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin. J Cell Biol 1992, 116:405-422.
    • (1992) J Cell Biol , vol.116 , pp. 405-422
    • Wice, B.M.1    Gordon, J.I.2
  • 46
    • 0006773266 scopus 로고
    • Caveolae and human disease: Functional roles in transcytosis, potocytosis, signalling, and cell polarity
    • Lisanti PL, Scherer PE, Tang Z, Kübler E, Koleske AJ, Sargiacomo M: Caveolae and human disease: functional roles in transcytosis, potocytosis, signalling, and cell polarity. Semin Dev Biol 1995, 6:47-58.
    • (1995) Semin Dev Biol , vol.6 , pp. 47-58
    • Lisanti, P.L.1    Scherer, P.E.2    Tang, Z.3    Kübler, E.4    Koleske, A.J.5    Sargiacomo, M.6
  • 47
    • 0030222108 scopus 로고    scopus 로고
    • Caveolae and caveolins
    • Parton RG: Caveolae and caveolins. Curr Opin Cell Biol 1996, 8:542-548. This review article is an interesting and careful summary of the data on caveolae and caveolins.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 542-548
    • Parton, R.G.1
  • 49
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • Dupree P, Parton RG, Raposo G, Kurzchalia TV, Simons K: Caveolae and sorting in the trans-Golgi network of epithelial cells. EMBO J 1993, 12:1597-1605.
    • (1993) EMBO J , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 50
    • 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, Simons K: VIP21, a 21-KD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J Cell Biol 1992, 118:1003-1014.
    • (1992) J Cell Biol , vol.118 , pp. 1003-1014
    • Kurzchalia, T.V.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 51
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra AM, Williamson E, Simons K, Parton RG: Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J Biol Chem 1994, 269:30745-30748.
    • (1994) J Biol Chem , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 52
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent resistant complexes in the absence of caveolae
    • Gorodinski A, Harris DA: Glycolipid-anchored proteins in neuroblastoma cells form detergent resistant complexes in the absence of caveolae. J Cell Biol 1995, 129:619-627.
    • (1995) J Cell Biol , vol.129 , pp. 619-627
    • Gorodinski, A.1    Harris, D.A.2
  • 53
    • 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, 269:1435-1439.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 54
    • 0028998554 scopus 로고
    • VIP21-caveolin, a membrane protein constituent of the caveolar coat, forms high molecular mass oligomers in vivo and in vitro
    • Monier S, Parton RG, Vogel F, Henske A, Kurzchalia T: VIP21-caveolin, a membrane protein constituent of the caveolar coat, forms high molecular mass oligomers in vivo and in vitro. Mol Biol Cell 1995, 6:911-927.
    • (1995) Mol Biol Cell , vol.6 , pp. 911-927
    • Monier, S.1    Parton, R.G.2    Vogel, F.3    Henske, A.4    Kurzchalia, T.5
  • 56
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues: Palmitoylation is not required for localization of caveolin to caveolae
    • Dietzen DJ, Hastings WR, Lublin DM: Caveolin is palmitoylated on multiple cysteine residues: palmitoylation is not required for localization of caveolin to caveolae. J Biol Chem 1995, 270:6838-6842.
    • (1995) J Biol Chem , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 57
    • 0030591426 scopus 로고    scopus 로고
    • Oligomerisation of VIP21 -caveolin in vitro is stabilized by long chain fatty acylation or cholesterol
    • Monier S, Dietzen DJ, Hastings WR, Lublin DM, Kurzchalia TV: Oligomerisation of VIP21 -caveolin in vitro is stabilized by long chain fatty acylation or cholesterol. FEBS Lett 1996, 388:143-149. This paper shows that palmitoylation or cholesterol binding may synergize with protein-protein interactions between the caveolin polypeptides in order to enable the formation of caveolin oligomers and their sequestration of rafts.
    • (1996) FEBS Lett , vol.388 , pp. 143-149
    • Monier, S.1    Dietzen, D.J.2    Hastings, W.R.3    Lublin, D.M.4    Kurzchalia, T.V.5
  • 58
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored receptor for 5-methyltetrahydrofolate
    • Rothberg K, Ying Y, Kamen A, Anderson RGW: Cholesterol controls the clustering of the glycophospholipid-anchored receptor for 5-methyltetrahydrofolate. J Cell Biol 1990, 111:2931-2938.
    • (1990) J Cell Biol , vol.111 , pp. 2931-2938
    • Rothberg, K.1    Ying, Y.2    Kamen, A.3    Anderson, R.G.W.4
  • 59
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer JE, Oh P, Pinney E, Allard J: Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J Cell Biol 1994, 127:1217-1232.
    • (1994) J Cell Biol , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 60
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21 -caveolin
    • Fra AM, Williamson E, Simons K, Parton RG: De novo formation of caveolae in lymphocytes by expression of VIP21 -caveolin. Proc Natl Acad Sci USA 1995, 92:8655-8659.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 61
    • 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, 376:108-112.
    • (1995) FEBS Lett , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 63
    • 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, 136:137-154. The subcellular localization of caveolin 3 was analyzed during myogenesis and in fully developed skeletal muscle. In fully differentiated skeletal muscle, caveolin 3 is restricted to the sarcolemmal caveolae. During the development of muscle, large grape-like clusters of caveolin-3-containirtg caveolae appear to be the starting point of T-tubule biogenesis. These findings suggest that caveolin 3 organizes large raft domains from which the highly specialized T tubules are generated.
    • (1997) J Cell Biol , vol.136 , pp. 137-154
    • Parton, R.G.1    Way, M.2    Zorzi, N.3    Stang, E.4
  • 64
    • 0028032064 scopus 로고
    • Caveolin/VIP21 and glycosphingolipid clusters in the sorting of glycosylphosphatidylinositol-anchored protein in epithelial cells
    • Zurzolo C, Van't Hof W, van Meer G, Rodriguez-Boulan E: Caveolin/VIP21 and glycosphingolipid clusters in the sorting of glycosylphosphatidylinositol-anchored protein in epithelial cells. EMBO J 1994, 13:42-53,
    • (1994) EMBO J , vol.13 , pp. 42-53
    • Zurzolo, C.1    Van't Hof, W.2    Van Meer, G.3    Rodriguez-Boulan, E.4
  • 65
    • 0029818694 scopus 로고    scopus 로고
    • Detergent-resistant membrane microdomains from CaCo-2 cells do not contain caveolin
    • Mirre C, Monlauzeur L, Garcia M, Delgrossi MH, Le Bivic A: Detergent-resistant membrane microdomains from CaCo-2 cells do not contain caveolin. Am J Physiol 1996, 271:C887-C894.
    • (1996) Am J Physiol , vol.271
    • Mirre, C.1    Monlauzeur, L.2    Garcia, M.3    Delgrossi, M.H.4    Le Bivic, A.5
  • 66
    • 0029757511 scopus 로고    scopus 로고
    • GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking
    • Fujimoto T: GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking. J Histochem Cytochem 1996, 44:929-941.
    • (1996) J Histochem Cytochem , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 67
    • 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, 264:1948-1951.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 68
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor S, Maxfield FR: Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment Mol Biol Cell 1995, 6:929-944,
    • (1995) Mol Biol Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 69
    • 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, 42:155-166.
    • (1994) J Histochem Cytochem , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 70
    • 0028981284 scopus 로고
    • lyn to detergent-resistant membrane domains accompanies cellular signaling
    • lyn to detergent-resistant membrane domains accompanies cellular signaling, Proc Natl Acad Sci USA 1995, 92:9201-9205.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9201-9205
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 72
    • 0028352175 scopus 로고
    • Urge-scale coaggregation of fluorescent lipid probes with cell surface proteins
    • Thomas JL, Holowka D, Baird B, Webb WW: Urge-scale coaggregation of fluorescent lipid probes with cell surface proteins. J Cell Biol 1994, 125:795-802.
    • (1994) J Cell Biol , vol.125 , pp. 795-802
    • Thomas, J.L.1    Holowka, D.2    Baird, B.3    Webb, W.W.4
  • 73
    • 0029665631 scopus 로고    scopus 로고
    • Fc epsilon RI-mediated association of 6-micron beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling
    • lyn increases. Moreover, a co-redistribution of raft lipid markers to the patches of the receptor was shown by fluorescence microscopy. These studies demonstrate that association of specific markers and of FceRI to raft microdomains is increased by clustering of FceRI.
    • (1996) J Cell Biol , vol.134 , pp. 1427-1439
    • Pierini, L.1    Holowka, D.2    Baird, B.3
  • 74
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with β-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein U, Gimpl G, Fahrenholz F: Alteration of the myometrial plasma membrane cholesterol content with β-cyclodextrin modulates the binding affinity of the oxytocin receptor, Biochemistry 1995, 34:13784-13793.
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 75
    • 0030753816 scopus 로고    scopus 로고
    • Lipid domains in the membrane: Thermotropic properties of sphingomyelin vesicles containing GM1 ganglioside and cholesterol
    • in press
    • Ferraretto A, Pitto M, Palestini P, Masserini M: Lipid domains in the membrane: thermotropic properties of sphingomyelin vesicles containing GM1 ganglioside and cholesterol. Biochemistry 1997, in press.
    • (1997) Biochemistry
    • Ferraretto, A.1    Pitto, M.2    Palestini, P.3    Masserini, M.4


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