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Volumn 16, Issue 4, 2004, Pages 373-378

Membrane lipids and vesicular traffic

Author keywords

endoplamsic reticulum; ER; glycosylphosphatidylinositol; GPI

Indexed keywords

AMINOPHOSPHOLIPID; LIPID BINDING PROTEIN; MEMBRANE LIPID; PHOSPHOLIPID; POLYPHOSPHOINOSITIDE; SPHINGOLIPID;

EID: 3142516233     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.06.004     Document Type: Review
Times cited : (155)

References (50)
  • 2
    • 0038662612 scopus 로고    scopus 로고
    • Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid
    • Kooijman E.E., Chupin V., de Kruijff B., Burger K.N. Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid. Traffic. 4:2003;162-174
    • (2003) Traffic , vol.4 , pp. 162-174
    • Kooijman, E.E.1    Chupin, V.2    De Kruijff, B.3    Burger, K.N.4
  • 3
    • 9144273746 scopus 로고    scopus 로고
    • Role of LBPA and Alix in multivesicular liposome formation and endosome organization
    • The biologically active 2,2′-stereoisomer of lysobisphosphatidic acid has the intrinsic capacity to drive vesicle budding and fission into acidified liposomes, a situation resembling late endosomal structures. Paradoxically, the cytosolic LBPA-binding protein Alix, also found in exosomes, inhibits invagination in vitro, but is required for the biogenesis of multivesicular endosomes in vivo.
    • Matsuo H., Chevallier J., Mayran N., Le Blanc I., Ferguson C., Faure J., Blanc N.S., Matile S., Dubochet J., Sadoul R., et al. Role of LBPA and Alix in multivesicular liposome formation and endosome organization. Science. 303:2004;531-534 The biologically active 2, 2′-stereoisomer of lysobisphosphatidic acid has the intrinsic capacity to drive vesicle budding and fission into acidified liposomes, a situation resembling late endosomal structures. Paradoxically, the cytosolic LBPA-binding protein Alix, also found in exosomes, inhibits invagination in vitro, but is required for the biogenesis of multivesicular endosomes in vivo.
    • (2004) Science , vol.303 , pp. 531-534
    • Matsuo, H.1    Chevallier, J.2    Mayran, N.3    Le Blanc, I.4    Ferguson, C.5    Faure, J.6    Blanc, N.S.7    Matile, S.8    Dubochet, J.9    Sadoul, R.10
  • 4
    • 0037423214 scopus 로고    scopus 로고
    • Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1
    • Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M. Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1. J Biol Chem. 278:2003;4160-4167
    • (2003) J Biol Chem , vol.278 , pp. 4160-4167
    • Modregger, J.1    Schmidt, A.A.2    Ritter, B.3    Huttner, W.B.4    Plomann, M.5
  • 6
    • 0344119435 scopus 로고    scopus 로고
    • Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: A theoretical model
    • Shemesh T., Luini A., Malhotra V., Burger K.N., Kozlov M.M. Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: a theoretical model. Biophys J. 85:2003;3813-3827
    • (2003) Biophys J , vol.85 , pp. 3813-3827
    • Shemesh, T.1    Luini, A.2    Malhotra, V.3    Burger, K.N.4    Kozlov, M.M.5
  • 7
    • 0032896265 scopus 로고    scopus 로고
    • Enhancement of endocytosis due to aminophospholipid transport across the plasma membrane of living cells
    • Farge E., Ojcius D.M., Subtil A., Dautry-Varsat A. Enhancement of endocytosis due to aminophospholipid transport across the plasma membrane of living cells. Am J Physiol. 276:1999;C725-C733
    • (1999) Am J Physiol , vol.276 , pp. 725-C733
    • Farge, E.1    Ojcius, D.M.2    Subtil, A.3    Dautry-Varsat, A.4
  • 8
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik L.V., Kozlov M.M. Protein-lipid interplay in fusion and fission of biological membranes. Annu Rev Biochem. 72:2003;175-207
    • (2003) Annu Rev Biochem , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 9
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • Baumgart T., Hess S.T., Webb W.W. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature. 425:2003;821-824
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 10
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • A thorough discussion of the limitations of the various methods to study lipid rafts. The author challenges cell biologists to develop adequate tools for assessing the existence of cellular rafts. Unfortunately, the compelling evidence on lipid sorting in vesicular traffic [31,32,43] does not receive proper credit from the author.
    • Munro S. Lipid rafts: elusive or illusive? Cell. 115:2003;377-388 A thorough discussion of the limitations of the various methods to study lipid rafts. The author challenges cell biologists to develop adequate tools for assessing the existence of cellular rafts. Unfortunately, the compelling evidence on lipid sorting in vesicular traffic [31, 32, 43] does not receive proper credit from the author.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 11
    • 0038650888 scopus 로고    scopus 로고
    • Dynamics of phosphoinositides in membrane retrieval and insertion
    • Czech M.P. Dynamics of phosphoinositides in membrane retrieval and insertion. Annu Rev Physiol. 65:2003;791-815
    • (2003) Annu Rev Physiol , vol.65 , pp. 791-815
    • Czech, M.P.1
  • 13
    • 0346756190 scopus 로고    scopus 로고
    • Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
    • Bigay J., Gounon P., Robineau S., Antonny B. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature. 426:2003;563-566
    • (2003) Nature , vol.426 , pp. 563-566
    • Bigay, J.1    Gounon, P.2    Robineau, S.3    Antonny, B.4
  • 14
    • 0344443667 scopus 로고    scopus 로고
    • Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum
    • Hua Z., Graham T.R. Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum. Mol Biol Cell. 14:2003;4971-4983
    • (2003) Mol Biol Cell , vol.14 , pp. 4971-4983
    • Hua, Z.1    Graham, T.R.2
  • 15
    • 0037345029 scopus 로고    scopus 로고
    • Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis
    • Pomorski T., Lombardi R., Riezman H., Devaux P.F., Van Meer G., Holthuis J.C. Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol Biol Cell. 14:2003;1240-1254
    • (2003) Mol Biol Cell , vol.14 , pp. 1240-1254
    • Pomorski, T.1    Lombardi, R.2    Riezman, H.3    Devaux, P.F.4    Van Meer, G.5    Holthuis, J.C.6
  • 16
    • 0842263750 scopus 로고    scopus 로고
    • Identification of a family of animal sphingomyelin synthases
    • •]) is a breakthrough in studies on sphingolipid metabolism and organization in the Golgi. Based on the prediction that the active center would be similar to that of the lipid phosphate phosphatase (LPP) family, the authors employ a functional cloning strategy in yeast to identify two mammalian sphingomyelin synthases, SMS1 in the Golgi and SMS2 at the plasma membrane, where it is presumably active in ceramide/diacylglycerol-mediated signaling events.
    • •]) is a breakthrough in studies on sphingolipid metabolism and organization in the Golgi. Based on the prediction that the active center would be similar to that of the lipid phosphate phosphatase (LPP) family, the authors employ a functional cloning strategy in yeast to identify two mammalian sphingomyelin synthases, SMS1 in the Golgi and SMS2 at the plasma membrane, where it is presumably active in ceramide/diacylglycerol-mediated signaling events.
    • (2004) EMBO J , vol.23 , pp. 33-44
    • Huitema, K.1    Van Den Dikkenberg, J.2    Brouwers, J.F.3    Holthuis, J.C.4
  • 17
    • 2442423192 scopus 로고    scopus 로고
    • Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin-synthase-defective lymphoid cells
    • •], SMS1 is cloned by expression cloning. Using a lymphoid cell line lacking SMS1, it is observed that SMS1 is required for growth under serum-free conditions.
    • •], SMS1 is cloned by expression cloning. Using a lymphoid cell line lacking SMS1, it is observed that SMS1 is required for growth under serum-free conditions.
    • (2004) J Biol Chem , vol.279 , pp. 18688-18693
    • Yamaoka, S.1    Miyaji, M.2    Kitano, T.3    Umehara, H.4    Okazaki, T.5
  • 20
    • 0037661715 scopus 로고    scopus 로고
    • Inhibition of a Golgi complex lysophospholipid acyltransferase induces membrane tubule formation and retrograde trafficking
    • Drecktrah D., Chambers K., Racoosin E.L., Cluett E.B., Gucwa A., Jackson B., Brown W.J. Inhibition of a Golgi complex lysophospholipid acyltransferase induces membrane tubule formation and retrograde trafficking. Mol Biol Cell. 14:2003;3459-3469
    • (2003) Mol Biol Cell , vol.14 , pp. 3459-3469
    • Drecktrah, D.1    Chambers, K.2    Racoosin, E.L.3    Cluett, E.B.4    Gucwa, A.5    Jackson, B.6    Brown, W.J.7
  • 21
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov O.O., Nichols B.J. Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat Cell Biol. 6:2004;238-243
    • (2004) Nat Cell Biol , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 22
    • 0037446837 scopus 로고    scopus 로고
    • GM1-containing lipid rafts are depleted within clathrin-coated pits
    • Nichols B.J. GM1-containing lipid rafts are depleted within clathrin-coated pits. Curr Biol. 13:2003;686-690
    • (2003) Curr Biol , vol.13 , pp. 686-690
    • Nichols, B.J.1
  • 24
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias D.A., Violin J.D., Newton A.C., Tsien R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 296:2002;913-916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 26
    • 0242268529 scopus 로고    scopus 로고
    • Cholesterol loading induces a block in the exit of VSVG from the TGN
    • Ying M., Grimmer S., Iversen T.G., Van Deurs B., Sandvig K. Cholesterol loading induces a block in the exit of VSVG from the TGN. Traffic. 4:2003;772-784
    • (2003) Traffic , vol.4 , pp. 772-784
    • Ying, M.1    Grimmer, S.2    Iversen, T.G.3    Van Deurs, B.4    Sandvig, K.5
  • 27
    • 0141642121 scopus 로고    scopus 로고
    • Sphingomyelin/phosphatidylcholine/cholesterol phase diagram: Boundaries and composition of lipid rafts
    • de Almeida R.F., Fedorov A., Prieto M. Sphingomyelin/phosphatidylcholine/ cholesterol phase diagram: boundaries and composition of lipid rafts. Biophys J. 85:2003;2406-2416
    • (2003) Biophys J , vol.85 , pp. 2406-2416
    • De Almeida, R.F.1    Fedorov, A.2    Prieto, M.3
  • 29
    • 0042780282 scopus 로고    scopus 로고
    • Mice lacking phosphatidylinositol transfer protein-α exhibit spinocerebellar degeneration, intestinal and hepatic steatosis, and hypoglycemia
    • Alb J.G. Jr., Cortese J.D., Phillips S.E., Albin R.L., Nagy T.R., Hamilton B.A., Bankaitis V.A. Mice lacking phosphatidylinositol transfer protein-α exhibit spinocerebellar degeneration, intestinal and hepatic steatosis, and hypoglycemia. J Biol Chem. 278:2003;33501-33518
    • (2003) J Biol Chem , vol.278 , pp. 33501-33518
    • Alb Jr., J.G.1    Cortese, J.D.2    Phillips, S.E.3    Albin, R.L.4    Nagy, T.R.5    Hamilton, B.A.6    Bankaitis, V.A.7
  • 32
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton R.G. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J Histochem Cytochem. 42:1994;155-166
    • (1994) J Histochem Cytochem , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 34
    • 0037470170 scopus 로고    scopus 로고
    • Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling
    • Sharma D.K., Choudhury A., Singh R.D., Wheatley C.L., Marks D.L., Pagano R.E. Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling. J Biol Chem. 278:2003;7564-7572
    • (2003) J Biol Chem , vol.278 , pp. 7564-7572
    • Sharma, D.K.1    Choudhury, A.2    Singh, R.D.3    Wheatley, C.L.4    Marks, D.L.5    Pagano, R.E.6
  • 36
    • 0038756797 scopus 로고    scopus 로고
    • Sphingolipid storage induces accumulation of intracellular cholesterol by stimulating SREBP-1 cleavage
    • Puri V., Jefferson J.R., Singh R.D., Wheatley C.L., Marks D.L., Pagano R.E. Sphingolipid storage induces accumulation of intracellular cholesterol by stimulating SREBP-1 cleavage. J Biol Chem. 278:2003;20961-20970
    • (2003) J Biol Chem , vol.278 , pp. 20961-20970
    • Puri, V.1    Jefferson, J.R.2    Singh, R.D.3    Wheatley, C.L.4    Marks, D.L.5    Pagano, R.E.6
  • 37
    • 10744221008 scopus 로고    scopus 로고
    • Niemann-Pick C1 Like 1 protein is critical for intestinal cholesterol absorption
    • Convincing evidence that this class of sterol-sensing-domain-containing proteins are involved in cholesterol transport. The challenge is to unravel their mechanism of action. Cholesterol may not be the primary substrate and other proteins (and lipids) may be involved. Mammalian sterol-sensing domains may actually sense sterols, whereas in flies such a domain recognizes a sterol-independent membrane property [46].
    • Altmann S.W., Davis H.R. Jr., Zhu L.J., Yao X., Hoos L.M., Tetzloff G., Iyer S.P., Maguire M., Golovko A., Zeng M., et al. Niemann-Pick C1 Like 1 protein is critical for intestinal cholesterol absorption. Science. 303:2004;1201-1204 Convincing evidence that this class of sterol-sensing-domain- containing proteins are involved in cholesterol transport. The challenge is to unravel their mechanism of action. Cholesterol may not be the primary substrate and other proteins (and lipids) may be involved. Mammalian sterol-sensing domains may actually sense sterols, whereas in flies such a domain recognizes a sterol-independent membrane property [46].
    • (2004) Science , vol.303 , pp. 1201-1204
    • Altmann, S.W.1    Davis Jr., H.R.2    Zhu, L.J.3    Yao, X.4    Hoos, L.M.5    Tetzloff, G.6    Iyer, S.P.7    Maguire, M.8    Golovko, A.9    Zeng, M.10
  • 39
    • 0037926403 scopus 로고    scopus 로고
    • Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells
    • Mayran N., Parton R.G., Gruenberg J. Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells. EMBO J. 22:2003;3242-3253
    • (2003) EMBO J , vol.22 , pp. 3242-3253
    • Mayran, N.1    Parton, R.G.2    Gruenberg, J.3
  • 40
    • 0344012479 scopus 로고    scopus 로고
    • The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes
    • Zobiack N., Rescher U., Ludwig C., Zeuschner D., Gerke V. The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes. Mol Biol Cell. 14:2003;4896-4908
    • (2003) Mol Biol Cell , vol.14 , pp. 4896-4908
    • Zobiack, N.1    Rescher, U.2    Ludwig, C.3    Zeuschner, D.4    Gerke, V.5
  • 42
    • 1542319939 scopus 로고    scopus 로고
    • Role of multiple drug resistance protein 1 in neutral but not acidic glycosphingolipid biosynthesis
    • De Rosa M.F., Sillence D., Ackerley C., Lingwood C. Role of multiple drug resistance protein 1 in neutral but not acidic glycosphingolipid biosynthesis. J Biol Chem. 279:2004;7867-7876
    • (2004) J Biol Chem , vol.279 , pp. 7867-7876
    • De Rosa, M.F.1    Sillence, D.2    Ackerley, C.3    Lingwood, C.4
  • 43
    • 0037414770 scopus 로고    scopus 로고
    • Trans-Golgi network and subapical compartment of HepG2 cells display different properties in sorting and exiting of sphingolipids
    • Maier O., Hoekstra D. Trans-Golgi network and subapical compartment of HepG2 cells display different properties in sorting and exiting of sphingolipids. J Biol Chem. 278:2003;164-173
    • (2003) J Biol Chem , vol.278 , pp. 164-173
    • Maier, O.1    Hoekstra, D.2
  • 44
    • 0038620205 scopus 로고    scopus 로고
    • Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway
    • Möbius W., van Donselaar E., Ohno-Iwashita Y., Shimada Y., Heijnen H.F., Slot J.W., Geuze H.J. Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic. 4:2003;222-231
    • (2003) Traffic , vol.4 , pp. 222-231
    • Möbius, W.1    Van Donselaar, E.2    Ohno-Iwashita, Y.3    Shimada, Y.4    Heijnen, H.F.5    Slot, J.W.6    Geuze, H.J.7
  • 46
    • 0041315472 scopus 로고    scopus 로고
    • Reconstitution of sterol-regulated endoplasmic reticulum-to-Golgi transport of SREBP-2 in insect cells by co-expression of mammalian SCAP and Insigs
    • Dobrosotskaya I.Y., Goldstein J.L., Brown M.S., Rawson R.B. Reconstitution of sterol-regulated endoplasmic reticulum-to-Golgi transport of SREBP-2 in insect cells by co-expression of mammalian SCAP and Insigs. J Biol Chem. 278:2003;35837-35843
    • (2003) J Biol Chem , vol.278 , pp. 35837-35843
    • Dobrosotskaya, I.Y.1    Goldstein, J.L.2    Brown, M.S.3    Rawson, R.B.4
  • 47
    • 1542379962 scopus 로고    scopus 로고
    • The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition
    • Brügger B., Graham C., Leibrecht I., Mombelli E., Jen A., Wieland F., Morris R. The membrane domains occupied by glycosylphosphatidylinositol- anchored prion protein and Thy-1 differ in lipid composition. J Biol Chem. 279:2004;7530-7536
    • (2004) J Biol Chem , vol.279 , pp. 7530-7536
    • Brügger, B.1    Graham, C.2    Leibrecht, I.3    Mombelli, E.4    Jen, A.5    Wieland, F.6    Morris, R.7
  • 48
    • 0346057912 scopus 로고    scopus 로고
    • Single-molecule imaging of the H-ras membrane-anchor reveals domains in the cytoplasmic leaflet of the cell membrane
    • Lommerse P.H., Blab G.A., Cognet L., Harms G.S., Snaar-Jagalska B.E., Spaink H.P., Schmidt T. Single-molecule imaging of the H-ras membrane-anchor reveals domains in the cytoplasmic leaflet of the cell membrane. Biophys J. 86:2004;609-616
    • (2004) Biophys J , vol.86 , pp. 609-616
    • Lommerse, P.H.1    Blab, G.A.2    Cognet, L.3    Harms, G.S.4    Snaar-Jagalska, B.E.5    Spaink, H.P.6    Schmidt, T.7


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