메뉴 건너뛰기




Volumn 78, Issue , 2009, Pages 827-856

Genetic and biochemical analysis of non-vesicular lipid traffic

Author keywords

Membranes; Phospholipids; Sphingolipids; Sterols; Transporters

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; BACTERIUM LIPOPOLYSACCHARIDE; CERAMIDE; CHOLESTEROL; GLUCOSYLCERAMIDE; GLYCEROPHOSPHOLIPID; GLYCOSPHINGOLIPID; PHOSPHATIDYLSERINE; PHOSPHOLIPID; SCRAMBLASE; SPHINGOLIPID; STEROL;

EID: 67650747650     PISSN: 00664154     EISSN: 00664154     Source Type: Book Series    
DOI: 10.1146/annurev.biochem.78.081307.112144     Document Type: Review
Times cited : (61)

References (140)
  • 3
    • 14644393694 scopus 로고    scopus 로고
    • Lipid traffic: Floppy drives and a superhighway
    • Holthuis JC, Levine TP. 2005. Lipid traffic: floppy drives and a superhighway. Nat. Rev. Mol. Cell Biol. 6:209-20
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 209-220
    • Holthuis, J.C.1    Levine, T.P.2
  • 4
    • 0036780197 scopus 로고    scopus 로고
    • Lasker Basic Medical Research Award. SEC mutants and the secretory apparatus
    • Schekman R. 2002. Lasker Basic Medical Research Award. SEC mutants and the secretory apparatus. Nat. Med. 8:1055-58
    • (2002) Nat. Med , vol.8 , pp. 1055-1058
    • Schekman, R.1
  • 5
    • 33645292025 scopus 로고    scopus 로고
    • Membrane microdomains, caveolae, and caveolar endocytosis of sphingolipids
    • Cheng ZJ, Singh RD, Marks DL, Pagano RE. 2006. Membrane microdomains, caveolae, and caveolar endocytosis of sphingolipids. Mol. Membr. Biol. 23:101-10
    • (2006) Mol. Membr. Biol , vol.23 , pp. 101-110
    • Cheng, Z.J.1    Singh, R.D.2    Marks, D.L.3    Pagano, R.E.4
  • 6
    • 33745635738 scopus 로고    scopus 로고
    • Distinct mechanisms of clathrinindependent endocytosis have unique sphingolipid requirements
    • Cheng ZJ, Singh RD, Sharma DK, Holicky EL, Hanada K, et al. 2006. Distinct mechanisms of clathrinindependent endocytosis have unique sphingolipid requirements. Mol. Biol. Cell 17:3197-210
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3197-3210
    • Cheng, Z.J.1    Singh, R.D.2    Sharma, D.K.3    Holicky, E.L.4    Hanada, K.5
  • 7
    • 0021099854 scopus 로고
    • Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane
    • Sleight RG, Pagano RE. 1983. Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane. J. Biol. Chem. 258:9050-58
    • (1983) J. Biol. Chem , vol.258 , pp. 9050-9058
    • Sleight, R.G.1    Pagano, R.E.2
  • 8
    • 0022416616 scopus 로고
    • Intracellular transport of phosphatidylcholine to the plasma membrane
    • Kaplan MR, Simoni RD. 1985. Intracellular transport of phosphatidylcholine to the plasma membrane. J. Cell Biol. 101:441-45
    • (1985) J. Cell Biol , vol.101 , pp. 441-445
    • Kaplan, M.R.1    Simoni, R.D.2
  • 9
    • 0025128087 scopus 로고
    • Characterization of phosphatidylserine synthesis and translocation in permeabilized animal cells
    • Voelker DR. 1990. Characterization of phosphatidylserine synthesis and translocation in permeabilized animal cells. J. Biol. Chem. 265:14340-46
    • (1990) J. Biol. Chem , vol.265 , pp. 14340-14346
    • Voelker, D.R.1
  • 10
    • 0025917178 scopus 로고
    • Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites for synthesis to the cell surface
    • Vance JE, Aasman EJ, Szarka R. 1991. Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites for synthesis to the cell surface. J. Biol. Chem. 266:8241-47
    • (1991) J. Biol. Chem , vol.266 , pp. 8241-8247
    • Vance, J.E.1    Aasman, E.J.2    Szarka, R.3
  • 11
    • 0035831459 scopus 로고    scopus 로고
    • Characterization of phosphatidylserine transport to the locus of phosphatidylserine decarboxylase 2 in permeabilized yeast
    • Wu WI, Voelker DR. 2001. Characterization of phosphatidylserine transport to the locus of phosphatidylserine decarboxylase 2 in permeabilized yeast. J. Biol. Chem. 276:7114-21
    • (2001) J. Biol. Chem , vol.276 , pp. 7114-7121
    • Wu, W.I.1    Voelker, D.R.2
  • 12
    • 0037185026 scopus 로고    scopus 로고
    • Phosphatidylserine transport to the mitochondria is regulated by ubiquitination
    • Schumacher MM, Choi JY, Voelker DR. 2002. Phosphatidylserine transport to the mitochondria is regulated by ubiquitination. J. Biol. Chem. 277:51033-42
    • (2002) J. Biol. Chem , vol.277 , pp. 51033-51042
    • Schumacher, M.M.1    Choi, J.Y.2    Voelker, D.R.3
  • 13
    • 33646227441 scopus 로고    scopus 로고
    • Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide
    • Hanada K. 2006. Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide. Mol. Cell Biochem. 286:23-31
    • (2006) Mol. Cell Biochem , vol.286 , pp. 23-31
    • Hanada, K.1
  • 15
    • 35348991132 scopus 로고    scopus 로고
    • Pre- and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis
    • Halter D, Neumann S, van Dijk SM, Wolthoorn J, de Maziere AM, et al. 2007. Pre- and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis. J. Cell Biol. 179:101-15
    • (2007) J. Cell Biol , vol.179 , pp. 101-115
    • Halter, D.1    Neumann, S.2    van Dijk, S.M.3    Wolthoorn, J.4    de Maziere, A.M.5
  • 16
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    • Raychaudhuri S, Im YJ, Hurley JH, Prinz WA. 2006. Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides. J. Cell Biol. 173:107-19
    • (2006) J. Cell Biol , vol.173 , pp. 107-119
    • Raychaudhuri, S.1    Im, Y.J.2    Hurley, J.H.3    Prinz, W.A.4
  • 17
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • Voelker DR. 2005. Bridging gaps in phospholipid transport. Trends Biochem. Sci. 30:396-404
    • (2005) Trends Biochem. Sci , vol.30 , pp. 396-404
    • Voelker, D.R.1
  • 18
    • 33746035655 scopus 로고    scopus 로고
    • Translocator protein (18 kDa): New nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function
    • Papadopoulos V, Baraldi M, Guilarte TR, Knudsen TB, Lacapere JJ, et al. 2006. Translocator protein (18 kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function. Trends Pharmacol. Sci. 27:402-9
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 402-409
    • Papadopoulos, V.1    Baraldi, M.2    Guilarte, T.R.3    Knudsen, T.B.4    Lacapere, J.J.5
  • 19
    • 0014409392 scopus 로고
    • Exchange of phospholipids between liver mitochondria and microsomes in vitro
    • Wirtz KW, Zilversmit DB. 1968. Exchange of phospholipids between liver mitochondria and microsomes in vitro. J. Biol. Chem. 243:3596-602
    • (1968) J. Biol. Chem , vol.243 , pp. 3596-3602
    • Wirtz, K.W.1    Zilversmit, D.B.2
  • 20
    • 33749079613 scopus 로고    scopus 로고
    • Phospholipid transfer proteins in perspective
    • Wirtz KW. 2006. Phospholipid transfer proteins in perspective. FEBS Lett. 580:5436-41
    • (2006) FEBS Lett , vol.580 , pp. 5436-5441
    • Wirtz, K.W.1
  • 21
    • 33749555280 scopus 로고    scopus 로고
    • Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT
    • Kawano M, Kumagai K, Nishijima M, Hanada K. 2006. Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT. J. Biol. Chem. 281:30279-88
    • (2006) J. Biol. Chem , vol.281 , pp. 30279-30288
    • Kawano, M.1    Kumagai, K.2    Nishijima, M.3    Hanada, K.4
  • 22
    • 34548498611 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide
    • D'Angelo G, Polishchuk E, Di Tullio G, Santoro M, Di Campli A, et al. 2007. Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature 449:62-67
    • (2007) Nature , vol.449 , pp. 62-67
    • D'Angelo, G.1    Polishchuk, E.2    Di Tullio, G.3    Santoro, M.4    Di Campli, A.5
  • 23
    • 1342346595 scopus 로고    scopus 로고
    • Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process
    • Wu WI, Voelker DR. 2004. Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process. J. Biol. Chem. 279:6635-42
    • (2004) J. Biol. Chem , vol.279 , pp. 6635-6642
    • Wu, W.I.1    Voelker, D.R.2
  • 24
    • 44449129087 scopus 로고    scopus 로고
    • Protein phosphatase 2Cepsilon is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes
    • Saito S, Matsui H, Kawano M, Kumagai K, Tomishige N, et al. 2008. Protein phosphatase 2Cepsilon is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes. J. Biol. Chem. 283:6584-93
    • (2008) J. Biol. Chem , vol.283 , pp. 6584-6593
    • Saito, S.1    Matsui, H.2    Kawano, M.3    Kumagai, K.4    Tomishige, N.5
  • 25
    • 34547096008 scopus 로고    scopus 로고
    • Interorganelle trafficking of ceramide is regulated by phosphorylation-dependent cooperativity between the PH and STARTdomains of CERT
    • Kumagai K, Kawano M, Shinkai-Ouchi F, Nishijima M, Hanada K. 2007. Interorganelle trafficking of ceramide is regulated by phosphorylation-dependent cooperativity between the PH and STARTdomains of CERT. J. Biol. Chem. 282:17758-66
    • (2007) J. Biol. Chem , vol.282 , pp. 17758-17766
    • Kumagai, K.1    Kawano, M.2    Shinkai-Ouchi, F.3    Nishijima, M.4    Hanada, K.5
  • 26
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Moller JV, Juul B, le Maire M. 1996. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286:1-51
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    le Maire, M.3
  • 27
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na, K-ATPase
    • Kaplan JH. 2002. Biochemistry of Na, K-ATPase. Annu. Rev. Biochem. 71:511-35
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 28
    • 0034717837 scopus 로고    scopus 로고
    • Identification and purification of aminophospholipid flippases
    • Daleke DL, Lyles JV. 2000. Identification and purification of aminophospholipid flippases. Biochim. Biophys. Acta 1486:108-27
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 108-127
    • Daleke, D.L.1    Lyles, J.V.2
  • 29
    • 0001505065 scopus 로고
    • ATP-dependent asymmetric distribution of spin-labeled phospholipids in the erythrocyte membrane: Relation to shape changes
    • Seigneuret M, Devaux PF. 1984. ATP-dependent asymmetric distribution of spin-labeled phospholipids in the erythrocyte membrane: relation to shape changes. Proc. Natl. Acad. Sci. USA 81:3751-55
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3751-3755
    • Seigneuret, M.1    Devaux, P.F.2
  • 30
    • 0022371311 scopus 로고
    • Incorporation and translocation of amino-phospholipids in human erythrocytes
    • Daleke DL, Huestis WH. 1985. Incorporation and translocation of amino-phospholipids in human erythrocytes. Biochemistry 24:5406-16
    • (1985) Biochemistry , vol.24 , pp. 5406-5416
    • Daleke, D.L.1    Huestis, W.H.2
  • 31
    • 0025780777 scopus 로고
    • Vanadate-sensitive ATPase from chromaffin granule membranes formed a phosphoenzyme intermediate and was activated by phosphatidylserine
    • Moriyama Y, Nelson N, Maeda M, Futai M. 1991. Vanadate-sensitive ATPase from chromaffin granule membranes formed a phosphoenzyme intermediate and was activated by phosphatidylserine. Arch. Biochem. Biophys. 286:252-56
    • (1991) Arch. Biochem. Biophys , vol.286 , pp. 252-256
    • Moriyama, Y.1    Nelson, N.2    Maeda, M.3    Futai, M.4
  • 32
    • 0023901094 scopus 로고
    • Purification and properties of a vanadate- and N-ethylmaleimide-sensitive ATPase from chromaffin granule membranes
    • Moriyama Y, Nelson N. 1988. Purification and properties of a vanadate- and N-ethylmaleimide-sensitive ATPase from chromaffin granule membranes. J. Biol. Chem. 263:8521-27
    • (1988) J. Biol. Chem , vol.263 , pp. 8521-8527
    • Moriyama, Y.1    Nelson, N.2
  • 33
    • 0029992825 scopus 로고    scopus 로고
    • A subfamily of P-type ATPases with aminophospholipid transporting activity
    • Tang X, Halleck MS, Schlegel RA, Williamson P. 1996. A subfamily of P-type ATPases with aminophospholipid transporting activity. Science 272:1495-97
    • (1996) Science , vol.272 , pp. 1495-1497
    • Tang, X.1    Halleck, M.S.2    Schlegel, R.A.3    Williamson, P.4
  • 34
    • 0032545424 scopus 로고    scopus 로고
    • Loss of Drs2p does not abolish transfer of fluorescence-labeled phospholipids across the plasma membrane of Saccharomyces cerevisiae
    • Siegmund A, Grant A, Angeletti C, Malone L, Nichols JW, Rudolph HK. 1998. Loss of Drs2p does not abolish transfer of fluorescence-labeled phospholipids across the plasma membrane of Saccharomyces cerevisiae. J. Biol. Chem. 273:34399-405
    • (1998) J. Biol. Chem , vol.273 , pp. 34399-34405
    • Siegmund, A.1    Grant, A.2    Angeletti, C.3    Malone, L.4    Nichols, J.W.5    Rudolph, H.K.6
  • 35
    • 0036732873 scopus 로고    scopus 로고
    • An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system
    • Hua Z, Fatheddin P, Graham TR. 2002. An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system. Mol. Biol. Cell 13:3162-77
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3162-3177
    • Hua, Z.1    Fatheddin, P.2    Graham, T.R.3
  • 36
    • 0033552605 scopus 로고    scopus 로고
    • Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function
    • Chen CY, Ingram MF, Rosal PH, Graham TR. 1999. Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. J. Cell Biol. 147:1223-36
    • (1999) J. Cell Biol , vol.147 , pp. 1223-1236
    • Chen, C.Y.1    Ingram, M.F.2    Rosal, P.H.3    Graham, T.R.4
  • 37
    • 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 PF, van Meer G, Holthuis JC. 2003. 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 14:1240-54
    • (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
  • 38
    • 9644264229 scopus 로고    scopus 로고
    • Flippases and vesicle-mediated protein transport
    • Graham TR. 2004. Flippases and vesicle-mediated protein transport. Trends Cell Biol. 14:670-77
    • (2004) Trends Cell Biol , vol.14 , pp. 670-677
    • Graham, T.R.1
  • 39
    • 0037020182 scopus 로고    scopus 로고
    • A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae
    • Kato U, Emoto K, Fredriksson C, Nakamura H, Ohta A, et al. 2002. A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae. J. Biol. Chem. 277:37855-62
    • (2002) J. Biol. Chem , vol.277 , pp. 37855-37862
    • Kato, U.1    Emoto, K.2    Fredriksson, C.3    Nakamura, H.4    Ohta, A.5
  • 40
    • 0141704333 scopus 로고    scopus 로고
    • Lem3p is essential for the uptake and potency of alkylphosphocholine drugs, edelfosin and miltefosine
    • Hanson P, Malone L, Birchmore J, Nichols JW. 2003. Lem3p is essential for the uptake and potency of alkylphosphocholine drugs, edelfosin and miltefosine. J. Biol. Chem. 278:36041-50
    • (2003) J. Biol. Chem , vol.278 , pp. 36041-36050
    • Hanson, P.1    Malone, L.2    Birchmore, J.3    Nichols, J.W.4
  • 41
    • 3042728119 scopus 로고    scopus 로고
    • Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae
    • Saito K, Fujimura-Kamada K, Furuta N, Kato U, Umeda M, Tanaka K. 2004. Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae. Mol. Biol. Cell 15:3418-32
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3418-3432
    • Saito, K.1    Fujimura-Kamada, K.2    Furuta, N.3    Kato, U.4    Umeda, M.5    Tanaka, K.6
  • 42
    • 0035423116 scopus 로고    scopus 로고
    • Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion
    • Kato M, Wickner W. 2001. Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion. EMBO J. 20:4035-40
    • (2001) EMBO J , vol.20 , pp. 4035-4040
    • Kato, M.1    Wickner, W.2
  • 43
    • 33845987531 scopus 로고    scopus 로고
    • Uptake and utilization of lyso-phosphatidylethanolamine by Saccharomyces cerevisiae
    • Riekhof WR, Voelker DR. 2006. Uptake and utilization of lyso-phosphatidylethanolamine by Saccharomyces cerevisiae. J. Biol. Chem. 281:36588-96
    • (2006) J. Biol. Chem , vol.281 , pp. 36588-36596
    • Riekhof, W.R.1    Voelker, D.R.2
  • 44
    • 35348954738 scopus 로고    scopus 로고
    • Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae
    • Riekhof WR, Wu J, Jones JL, Voelker DR. 2007. Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 282:28344-52
    • (2007) J. Biol. Chem , vol.282 , pp. 28344-28352
    • Riekhof, W.R.1    Wu, J.2    Jones, J.L.3    Voelker, D.R.4
  • 45
    • 37549003679 scopus 로고    scopus 로고
    • Lyso-phosphatidylcholine metabolism in Saccharomyces cerevisiae. The role of P-type ATPases in transport and a broad specificity acyltransferase in acylation
    • Riekhof WR, Wu J, Gijon MA, Zarini S, Murphy RC, Voelker DR. 2007. Lyso-phosphatidylcholine metabolism in Saccharomyces cerevisiae. The role of P-type ATPases in transport and a broad specificity acyltransferase in acylation. J. Biol. Chem. 282:36853-61
    • (2007) J. Biol. Chem , vol.282 , pp. 36853-36861
    • Riekhof, W.R.1    Wu, J.2    Gijon, M.A.3    Zarini, S.4    Murphy, R.C.5    Voelker, D.R.6
  • 46
    • 28844471880 scopus 로고    scopus 로고
    • Fluorescent, acyl chain-labeled phosphatidylcholine analogs reveal novel transport pathways across the plasma membrane of yeast
    • Elvington SM, Bu F, Nichols JW. 2005. Fluorescent, acyl chain-labeled phosphatidylcholine analogs reveal novel transport pathways across the plasma membrane of yeast. J. Biol. Chem. 280:40957-64
    • (2005) J. Biol. Chem , vol.280 , pp. 40957-40964
    • Elvington, S.M.1    Bu, F.2    Nichols, J.W.3
  • 47
    • 33745413294 scopus 로고    scopus 로고
    • Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles
    • Alder-Baerens N, Lisman Q, Luong L, Pomorski T, Holthuis JC. 2006. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17:1632-42
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1632-1642
    • Alder-Baerens, N.1    Lisman, Q.2    Luong, L.3    Pomorski, T.4    Holthuis, J.C.5
  • 48
    • 3242669517 scopus 로고    scopus 로고
    • Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function
    • Natarajan P, Wang J, Hua Z, Graham TR. 2004. Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function. Proc. Natl. Acad. Sci. USA 101:10614-19
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10614-10619
    • Natarajan, P.1    Wang, J.2    Hua, Z.3    Graham, T.R.4
  • 50
    • 0031907132 scopus 로고    scopus 로고
    • A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis
    • Bull LN, van Eijk MJ, Pawlikowska L, DeYoung JA, Juijn JA, et al. 1998. A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat. Genet. 18:219-24
    • (1998) Nat. Genet , vol.18 , pp. 219-224
    • Bull, L.N.1    van Eijk, M.J.2    Pawlikowska, L.3    DeYoung, J.A.4    Juijn, J.A.5
  • 51
    • 0034812920 scopus 로고    scopus 로고
    • Familial intrahepatic cholestasis 1: Studies of localization and function
    • Ujhazy P, Ortiz D, Misra S, Li S, Moseley J, et al. 2001. Familial intrahepatic cholestasis 1: studies of localization and function. Hepatology 34:768-75
    • (2001) Hepatology , vol.34 , pp. 768-775
    • Ujhazy, P.1    Ortiz, D.2    Misra, S.3    Li, S.4    Moseley, J.5
  • 52
    • 38649113883 scopus 로고    scopus 로고
    • ATP8B1 requires an accessory protein for endoplasmic reticulum exit and plasma membrane lipid flippase activity
    • Paulusma CC, Folmer DE, Ho-Mok KS, de Waart DR, Hilarius PM, et al. 2008. ATP8B1 requires an accessory protein for endoplasmic reticulum exit and plasma membrane lipid flippase activity. Hepatology 47:268-78
    • (2008) Hepatology , vol.47 , pp. 268-278
    • Paulusma, C.C.1    Folmer, D.E.2    Ho-Mok, K.S.3    de Waart, D.R.4    Hilarius, P.M.5
  • 53
    • 33745906532 scopus 로고    scopus 로고
    • Atp8b1 deficiency in mice reduces resistance of the canalicular membrane to hydrophobic bile salts and impairs bile salt transport
    • Paulusma CC, Groen A, Kunne C, Ho-Mok KS, Spijkerboer AL, et al. 2006. Atp8b1 deficiency in mice reduces resistance of the canalicular membrane to hydrophobic bile salts and impairs bile salt transport. Hepatology 44:195-204
    • (2006) Hepatology , vol.44 , pp. 195-204
    • Paulusma, C.C.1    Groen, A.2    Kunne, C.3    Ho-Mok, K.S.4    Spijkerboer, A.L.5
  • 54
    • 0035853703 scopus 로고    scopus 로고
    • An Escherichia coli mutant defective in lipid export
    • Doerrler WT, Reedy MC, Raetz CR. 2001. An Escherichia coli mutant defective in lipid export. J. Biol. Chem. 276:11461-64
    • (2001) J. Biol. Chem , vol.276 , pp. 11461-11464
    • Doerrler, W.T.1    Reedy, M.C.2    Raetz, C.R.3
  • 55
    • 33645836299 scopus 로고    scopus 로고
    • Lipid trafficking to the outer membrane of gram-negative bacteria
    • Doerrler WT. 2006. Lipid trafficking to the outer membrane of gram-negative bacteria. Mol. Microbiol. 60:542-52
    • (2006) Mol. Microbiol , vol.60 , pp. 542-552
    • Doerrler, W.T.1
  • 56
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward A, Reyes CL, Yu J, Roth CB, Chang G. 2007. Flexibility in the ABC transporter MsbA: alternating access with a twist. Proc. Natl. Acad. Sci. USA 104:19005-10
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 58
    • 0037031860 scopus 로고    scopus 로고
    • Transcriptional profiling identifies two members of the ATP-binding cassette transporter superfamily required for sterol uptake in yeast
    • Wilcox LJ, Balderes DA, Wharton B, Tinkelenberg AH, Rao G, Sturley SL. 2002. Transcriptional profiling identifies two members of the ATP-binding cassette transporter superfamily required for sterol uptake in yeast. J. Biol. Chem. 277:32466-72
    • (2002) J. Biol. Chem , vol.277 , pp. 32466-32472
    • Wilcox, L.J.1    Balderes, D.A.2    Wharton, B.3    Tinkelenberg, A.H.4    Rao, G.5    Sturley, S.L.6
  • 59
    • 0345791510 scopus 로고    scopus 로고
    • Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein
    • Abe-Dohmae S, Ikeda Y, Matsuo M, Hayashi M, Okuhira K, et al. 2004. Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein. J. Biol. Chem. 279:604-11
    • (2004) J. Biol. Chem , vol.279 , pp. 604-611
    • Abe-Dohmae, S.1    Ikeda, Y.2    Matsuo, M.3    Hayashi, M.4    Okuhira, K.5
  • 60
    • 0032813809 scopus 로고    scopus 로고
    • The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease
    • Bodzioch M, Orso E, Klucken J, Langmann T, Bottcher A, et al. 1999. The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease. Nat. Genet. 22:347-51
    • (1999) Nat. Genet , vol.22 , pp. 347-351
    • Bodzioch, M.1    Orso, E.2    Klucken, J.3    Langmann, T.4    Bottcher, A.5
  • 61
    • 0032813808 scopus 로고    scopus 로고
    • Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency
    • Brooks-Wilson A, Marcil M, Clee SM, Zhang LH, Roomp K, et al. 1999. Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency. Nat. Genet. 22:336-45
    • (1999) Nat. Genet , vol.22 , pp. 336-345
    • Brooks-Wilson, A.1    Marcil, M.2    Clee, S.M.3    Zhang, L.H.4    Roomp, K.5
  • 62
    • 1642547065 scopus 로고    scopus 로고
    • ABCA1 mediates concurrent cholesterol and phospholipid efflux to apolipoprotein A-I
    • Smith JD, Le Goff W, Settle M, Brubaker G, Waelde C, et al. 2004. ABCA1 mediates concurrent cholesterol and phospholipid efflux to apolipoprotein A-I. J. Lipid Res. 45:635-44
    • (2004) J. Lipid Res , vol.45 , pp. 635-644
    • Smith, J.D.1    Le Goff, W.2    Settle, M.3    Brubaker, G.4    Waelde, C.5
  • 63
    • 34447531005 scopus 로고    scopus 로고
    • Enhanced apoA-I-dependent cholesterol efflux by ABCA1 from sphingomyelin-deficient Chinese hamster ovary cells
    • Nagao K, Takahashi K, Hanada K, Kioka N, Matsuo M, Ueda K. 2007. Enhanced apoA-I-dependent cholesterol efflux by ABCA1 from sphingomyelin-deficient Chinese hamster ovary cells. J. Biol. Chem. 282:14868-74
    • (2007) J. Biol. Chem , vol.282 , pp. 14868-14874
    • Nagao, K.1    Takahashi, K.2    Hanada, K.3    Kioka, N.4    Matsuo, M.5    Ueda, K.6
  • 64
    • 0142042380 scopus 로고    scopus 로고
    • ABCA1 redistributes membrane cholesterol independent of apolipoprotein interactions
    • Vaughan AM, Oram JF. 2003. ABCA1 redistributes membrane cholesterol independent of apolipoprotein interactions. J. Lipid Res. 44:1373-80
    • (2003) J. Lipid Res , vol.44 , pp. 1373-1380
    • Vaughan, A.M.1    Oram, J.F.2
  • 66
    • 34548364160 scopus 로고    scopus 로고
    • Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles
    • Vedhachalam C, Duong PT, Nickel M, Nguyen D, Dhanasekaran P, et al. 2007. Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles. J. Biol. Chem. 282:25123-30
    • (2007) J. Biol. Chem , vol.282 , pp. 25123-25130
    • Vedhachalam, C.1    Duong, P.T.2    Nickel, M.3    Nguyen, D.4    Dhanasekaran, P.5
  • 68
    • 0035900369 scopus 로고    scopus 로고
    • ABCA3is a lamellar body membrane protein in human lung alveolar type II cells
    • Yamano G, Funahashi H, Kawanami O, Zhao LX, Ban N, et al. 2001. ABCA3is a lamellar body membrane protein in human lung alveolar type II cells. FEBS Lett. 508:221-25
    • (2001) FEBS Lett , vol.508 , pp. 221-225
    • Yamano, G.1    Funahashi, H.2    Kawanami, O.3    Zhao, L.X.4    Ban, N.5
  • 71
    • 34548231083 scopus 로고    scopus 로고
    • ABCA3 is critical for lamellar body biogenesis in vivo
    • Cheong N, Zhang H, Madesh M, Zhao M, Yu K, et al. 2007. ABCA3 is critical for lamellar body biogenesis in vivo. J. Biol. Chem. 282:23811-17
    • (2007) J. Biol. Chem , vol.282 , pp. 23811-23817
    • Cheong, N.1    Zhang, H.2    Madesh, M.3    Zhao, M.4    Yu, K.5
  • 72
    • 34248205311 scopus 로고    scopus 로고
    • ABCA3 as a lipid transporter in pulmonary surfactant biogenesis
    • Ban N, Matsumura Y, Sakai H, Takanezawa Y, Sasaki M, et al. 2007. ABCA3 as a lipid transporter in pulmonary surfactant biogenesis. J. Biol. Chem. 282:9628-34
    • (2007) J. Biol. Chem , vol.282 , pp. 9628-9634
    • Ban, N.1    Matsumura, Y.2    Sakai, H.3    Takanezawa, Y.4    Sasaki, M.5
  • 73
    • 11144240503 scopus 로고    scopus 로고
    • N-retinylidene- phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR)
    • Beharry S, Zhong M, Molday RS. 2004. N-retinylidene- phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR). J. Biol. Chem. 279:53972-79
    • (2004) J. Biol. Chem , vol.279 , pp. 53972-53979
    • Beharry, S.1    Zhong, M.2    Molday, R.S.3
  • 74
    • 0031037951 scopus 로고    scopus 로고
    • A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy
    • Allikmets R, Singh N, Sun H, Shroyer NF, Hutchinson A, et al. 1997. A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy. Nat. Genet. 15:236-46
    • (1997) Nat. Genet , vol.15 , pp. 236-246
    • Allikmets, R.1    Singh, N.2    Sun, H.3    Shroyer, N.F.4    Hutchinson, A.5
  • 75
    • 0033794871 scopus 로고    scopus 로고
    • Simple and complex ABCR: Genetic predisposition to retinal disease
    • Allikmets R. 2000. Simple and complex ABCR: genetic predisposition to retinal disease. Am. J. Hum. Genet. 67:793-99
    • (2000) Am. J. Hum. Genet , vol.67 , pp. 793-799
    • Allikmets, R.1
  • 76
    • 0027363563 scopus 로고
    • Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease
    • Smit JJ, Schinkel AH, Oude Elferink RP, Wagenaar E, van Deemter L, et al. 1993. Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease. Cell 75:451-62
    • (1993) Cell , vol.75 , pp. 451-462
    • Smit, J.J.1    Schinkel, A.H.2    Oude Elferink, R.P.3    Wagenaar, E.4    van Deemter, L.5
  • 77
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • Ruetz S, Gros P. 1994. Phosphatidylcholine translocase: a physiological role for the mdr2 gene. Cell 77:1071-81
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 79
    • 33847064667 scopus 로고    scopus 로고
    • MDR3 (ABCB4) defects: A paradigm for the genetics of adult cholestatic syndromes
    • Trauner M, Fickert P, Wagner M. 2007. MDR3 (ABCB4) defects: a paradigm for the genetics of adult cholestatic syndromes. Semin. Liver Dis. 27:77-98
    • (2007) Semin. Liver Dis , vol.27 , pp. 77-98
    • Trauner, M.1    Fickert, P.2    Wagner, M.3
  • 81
    • 33749385907 scopus 로고    scopus 로고
    • Deletion of the transmembrane transporter ABCG1 results in progressive pulmonary lipidosis
    • Baldan A, Tarr P, Vales CS, Frank J, Shimotake TK, et al. 2006. Deletion of the transmembrane transporter ABCG1 results in progressive pulmonary lipidosis. J. Biol. Chem. 281:29401-10
    • (2006) J. Biol. Chem , vol.281 , pp. 29401-29410
    • Baldan, A.1    Tarr, P.2    Vales, C.S.3    Frank, J.4    Shimotake, T.K.5
  • 82
    • 49149099266 scopus 로고    scopus 로고
    • Loss of ABCG1 results in chronic pulmonary inflammation
    • Baldan A, Gomes AV, Ping P, Edwards PA. 2008. Loss of ABCG1 results in chronic pulmonary inflammation. J. Immunol. 180:3560-68
    • (2008) J. Immunol , vol.180 , pp. 3560-3568
    • Baldan, A.1    Gomes, A.V.2    Ping, P.3    Edwards, P.A.4
  • 83
    • 44849094986 scopus 로고    scopus 로고
    • A critical role for ABCG1 in macrophage inflammation and lung homeostasis
    • Wojcik AJ, Skaflen MD, Srinivasan S, Hedrick CC. 2008. A critical role for ABCG1 in macrophage inflammation and lung homeostasis. J. Immunol. 180:4273-82
    • (2008) J. Immunol , vol.180 , pp. 4273-4282
    • Wojcik, A.J.1    Skaflen, M.D.2    Srinivasan, S.3    Hedrick, C.C.4
  • 84
    • 42049122331 scopus 로고    scopus 로고
    • ATP-binding cassette transporters G1 and G4 mediate cholesterol and desmosterol efflux to HDL and regulate sterol accumulation in the brain
    • Wang N, Yvan-Charvet L, Lutjohann D, Mulder M, Vanmierlo T, et al. 2008. ATP-binding cassette transporters G1 and G4 mediate cholesterol and desmosterol efflux to HDL and regulate sterol accumulation in the brain. FASEB J. 22:1073-82
    • (2008) FASEB J , vol.22 , pp. 1073-1082
    • Wang, N.1    Yvan-Charvet, L.2    Lutjohann, D.3    Mulder, M.4    Vanmierlo, T.5
  • 85
    • 17744390348 scopus 로고    scopus 로고
    • Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters
    • Berge KE, Tian H, Graf GA, Yu L, Grishin NV, et al. 2000. Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters. Science 290:1771-75
    • (2000) Science , vol.290 , pp. 1771-1775
    • Berge, K.E.1    Tian, H.2    Graf, G.A.3    Yu, L.4    Grishin, N.V.5
  • 86
    • 33748758161 scopus 로고    scopus 로고
    • Sterol transfer by ABCG5 and ABCG8: In vitro assay and reconstitution
    • Wang J, Sun F, Zhang DW, Ma Y, Xu F, et al. 2006. Sterol transfer by ABCG5 and ABCG8: in vitro assay and reconstitution. J. Biol. Chem. 281:27894-904
    • (2006) J. Biol. Chem , vol.281 , pp. 27894-27904
    • Wang, J.1    Sun, F.2    Zhang, D.W.3    Ma, Y.4    Xu, F.5
  • 87
    • 42949168278 scopus 로고    scopus 로고
    • Purification and reconstitution of sterol transfer by native mouse ABCG5 and ABCG8
    • Wang J, Zhang DW, Lei Y, Xu F, Cohen JC, et al. 2008. Purification and reconstitution of sterol transfer by native mouse ABCG5 and ABCG8. Biochemistry 47:5194-204
    • (2008) Biochemistry , vol.47 , pp. 5194-5204
    • Wang, J.1    Zhang, D.W.2    Lei, Y.3    Xu, F.4    Cohen, J.C.5
  • 88
    • 0026610874 scopus 로고
    • Ca2+ induces transbilayer redistribution of all major phospholipids in human erythrocytes
    • Williamson P, Kulick A, Zachowski A, Schlegel RA, Devaux PF. 1992. Ca2+ induces transbilayer redistribution of all major phospholipids in human erythrocytes. Biochemistry 31:6355-60
    • (1992) Biochemistry , vol.31 , pp. 6355-6360
    • Williamson, P.1    Kulick, A.2    Zachowski, A.3    Schlegel, R.A.4    Devaux, P.F.5
  • 90
    • 0034738623 scopus 로고    scopus 로고
    • Identification of three new members of the phospholipid scramblase gene family
    • Wiedmer T, Zhou Q, Kwoh DY, Sims PJ. 2000. Identification of three new members of the phospholipid scramblase gene family. Biochim. Biophys. Acta 1467:244-53
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 244-253
    • Wiedmer, T.1    Zhou, Q.2    Kwoh, D.Y.3    Sims, P.J.4
  • 91
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok VA, Voelker DR, Campbell PA, Cohen JJ, Bratton DL, Henson PM. 1992. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148:2207-16
    • (1992) J. Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 93
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green DR, Evan GI. 2002. A matter of life and death. Cancer Cell 1:19-30
    • (2002) Cancer Cell , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 94
    • 0036624776 scopus 로고    scopus 로고
    • Normal hemostasis but defective hematopoietic response to growth factors in mice deficient in phospholipid scramblase 1
    • Zhou Q, Zhao J, Wiedmer T, Sims PJ. 2002. Normal hemostasis but defective hematopoietic response to growth factors in mice deficient in phospholipid scramblase 1. Blood 99:4030-38
    • (2002) Blood , vol.99 , pp. 4030-4038
    • Zhou, Q.1    Zhao, J.2    Wiedmer, T.3    Sims, P.J.4
  • 95
    • 34547743049 scopus 로고    scopus 로고
    • Two alternative mechanisms that regulate the presentation of apoptotic cell engulfment signal in Caenorhabditis elegans
    • Venegas V, Zhou Z. 2007. Two alternative mechanisms that regulate the presentation of apoptotic cell engulfment signal in Caenorhabditis elegans. Mol. Biol. Cell 18:3180-92
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3180-3192
    • Venegas, V.1    Zhou, Z.2
  • 96
    • 34247862351 scopus 로고    scopus 로고
    • Wang X, Wang J, Gengyo-Ando K, Gu L, Sun CL, et al. 2007. C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1. Nat. Cell Biol. 9:541-49
    • Wang X, Wang J, Gengyo-Ando K, Gu L, Sun CL, et al. 2007. C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1. Nat. Cell Biol. 9:541-49
  • 97
    • 42049102578 scopus 로고    scopus 로고
    • Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis
    • Liu J, Epand RF, Durrant D, Grossman D, Chi NW, et al. 2008. Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis. Biochemistry 47:4518-29
    • (2008) Biochemistry , vol.47 , pp. 4518-4529
    • Liu, J.1    Epand, R.F.2    Durrant, D.3    Grossman, D.4    Chi, N.W.5
  • 98
    • 46549087800 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3
    • Ndebele K, Gona P, Jin TG, Benhaga N, Chalah A, et al. 2008. Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3. Apoptosis 13:845-56
    • (2008) Apoptosis , vol.13 , pp. 845-856
    • Ndebele, K.1    Gona, P.2    Jin, T.G.3    Benhaga, N.4    Chalah, A.5
  • 99
    • 4944230810 scopus 로고    scopus 로고
    • Intracellular trafficking of Niemann-Pick C proteins 1 and 2: Obligate components of subcellular lipid transport
    • Liscum L, Sturley SL. 2004. Intracellular trafficking of Niemann-Pick C proteins 1 and 2: obligate components of subcellular lipid transport. Biochim. Biophys. Acta 1685:22-27
    • (2004) Biochim. Biophys. Acta , vol.1685 , pp. 22-27
    • Liscum, L.1    Sturley, S.L.2
  • 100
    • 0034637440 scopus 로고    scopus 로고
    • Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein
    • Davies JP, Ioannou YA. 2000. Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein. J. Biol. Chem. 275:24367-74
    • (2000) J. Biol. Chem , vol.275 , pp. 24367-24374
    • Davies, J.P.1    Ioannou, Y.A.2
  • 102
    • 38149068309 scopus 로고    scopus 로고
    • Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop
    • Infante RE, Radhakrishnan A, Abi-Mosleh L, Kinch LN, Wang ML, et al. 2008. Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop. J. Biol. Chem. 283:1064-75
    • (2008) J. Biol. Chem , vol.283 , pp. 1064-1075
    • Infante, R.E.1    Radhakrishnan, A.2    Abi-Mosleh, L.3    Kinch, L.N.4    Wang, M.L.5
  • 103
    • 0034704245 scopus 로고    scopus 로고
    • Identification of HE1 as the second gene of Niemann-Pick C disease
    • Naureckiene S, Sleat DE, Lackland H, Fensom A, Vanier MT, et al. 2000. Identification of HE1 as the second gene of Niemann-Pick C disease. Science 290:2298-301
    • (2000) Science , vol.290 , pp. 2298-2301
    • Naureckiene, S.1    Sleat, D.E.2    Lackland, H.3    Fensom, A.4    Vanier, M.T.5
  • 104
    • 33750318425 scopus 로고    scopus 로고
    • Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport
    • Cheruku SR, Xu Z, Dutia R, Lobel P, Storch J. 2006. Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport. J. Biol. Chem. 281:31594-604
    • (2006) J. Biol. Chem , vol.281 , pp. 31594-31604
    • Cheruku, S.R.1    Xu, Z.2    Dutia, R.3    Lobel, P.4    Storch, J.5
  • 105
    • 34548192003 scopus 로고    scopus 로고
    • Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease
    • Xu S, Benoff B, Liou HL, Lobel P, Stock AM. 2007. Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease. J. Biol. Chem. 282:23525-31
    • (2007) J. Biol. Chem , vol.282 , pp. 23525-23531
    • Xu, S.1    Benoff, B.2    Liou, H.L.3    Lobel, P.4    Stock, A.M.5
  • 106
    • 0034655917 scopus 로고    scopus 로고
    • Evidence for a Niemann-Pick C (NPC) gene family: Identification and characterization of NPC1L1
    • Davies JP, Levy B, Ioannou YA. 2000. Evidence for a Niemann-Pick C (NPC) gene family: identification and characterization of NPC1L1. Genomics 65:137-45
    • (2000) Genomics , vol.65 , pp. 137-145
    • Davies, J.P.1    Levy, B.2    Ioannou, Y.A.3
  • 107
    • 3242668095 scopus 로고    scopus 로고
    • Direct binding of cholesterol to the purified membrane region of SCAP: Mechanism for a sterol-sensing domain
    • Radhakrishnan A, Sun LP, Kwon HJ, Brown MS, Goldstein JL. 2004. Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain. Mol. Cell 15:259-68
    • (2004) Mol. Cell , vol.15 , pp. 259-268
    • Radhakrishnan, A.1    Sun, L.P.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 109
    • 0034704244 scopus 로고    scopus 로고
    • Davies JP, Chen FW, Ioannou YA. 2000. Transmembrane molecular pump activity of Niemann-Pick C1 protein. Science 290:2295-98
    • Davies JP, Chen FW, Ioannou YA. 2000. Transmembrane molecular pump activity of Niemann-Pick C1 protein. Science 290:2295-98
  • 110
    • 44349126634 scopus 로고    scopus 로고
    • The cholesterol absorption inhibitor ezetimibe acts by blocking the sterol-induced internalization of NPC1L1
    • Ge L, Wang J, Qi W, Miao HH, Cao J, et al. 2008. The cholesterol absorption inhibitor ezetimibe acts by blocking the sterol-induced internalization of NPC1L1. Cell Metab. 7:508-19
    • (2008) Cell Metab , vol.7 , pp. 508-519
    • Ge, L.1    Wang, J.2    Qi, W.3    Miao, H.H.4    Cao, J.5
  • 111
    • 33845950113 scopus 로고    scopus 로고
    • Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli
    • Sperandeo P, Cescutti R, Villa R, Di Benedetto C, Candia D, et al. 2007. Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli. J. Bacteriol. 189:244-53
    • (2007) J. Bacteriol , vol.189 , pp. 244-253
    • Sperandeo, P.1    Cescutti, R.2    Villa, R.3    Di Benedetto, C.4    Candia, D.5
  • 112
    • 46049106143 scopus 로고    scopus 로고
    • Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Sperandeo P, Lau FK, Carpentieri A, De Castro C, Molinaro A, et al. 2008. Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli. J. Bacteriol. 190:4460-69
    • (2008) J. Bacteriol , vol.190 , pp. 4460-4469
    • Sperandeo, P.1    Lau, F.K.2    Carpentieri, A.3    De Castro, C.4    Molinaro, A.5
  • 113
    • 44449176988 scopus 로고    scopus 로고
    • Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Ruiz N, Gronenberg LS, Kahne D, Silhavy TJ. 2008. Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 105:5537-42
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5537-5542
    • Ruiz, N.1    Gronenberg, L.S.2    Kahne, D.3    Silhavy, T.J.4
  • 114
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu T, McCandlish AC, Gronenberg LS, Chng SS, Silhavy TJ, Kahne D. 2006. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 103:11754-59
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.S.4    Silhavy, T.J.5    Kahne, D.6
  • 115
    • 51749125875 scopus 로고    scopus 로고
    • Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis
    • Suits MD, Sperandeo P, Deho G, Polissi A, Jia Z. 2008. Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis. J. Mol. Biol. 380:476-88
    • (2008) J. Mol. Biol , vol.380 , pp. 476-488
    • Suits, M.D.1    Sperandeo, P.2    Deho, G.3    Polissi, A.4    Jia, Z.5
  • 116
    • 0036512409 scopus 로고    scopus 로고
    • Galactolipids rule in seed plants
    • Dormann P, Benning C. 2002. Galactolipids rule in seed plants. Trends Plant Sci. 7:112-18
    • (2002) Trends Plant Sci , vol.7 , pp. 112-118
    • Dormann, P.1    Benning, C.2
  • 117
    • 0038242363 scopus 로고    scopus 로고
    • A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis
    • Xu C, Fan J, Riekhof W, Froehlich JE, Benning C. 2003. A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis. EMBO J. 22:2370-79
    • (2003) EMBO J , vol.22 , pp. 2370-2379
    • Xu, C.1    Fan, J.2    Riekhof, W.3    Froehlich, J.E.4    Benning, C.5
  • 118
    • 33646004283 scopus 로고    scopus 로고
    • Mutation of the TGD1 chloroplast envelope protein affects phosphatidate metabolism in Arabidopsis
    • Xu C, Fan J, Froehlich JE, Awai K, Benning C. 2005. Mutation of the TGD1 chloroplast envelope protein affects phosphatidate metabolism in Arabidopsis. Plant Cell 17:3094-110
    • (2005) Plant Cell , vol.17 , pp. 3094-3110
    • Xu, C.1    Fan, J.2    Froehlich, J.E.3    Awai, K.4    Benning, C.5
  • 119
    • 33746096540 scopus 로고    scopus 로고
    • A phosphatidic acid-binding protein of the chloroplast inner envelope membrane involved in lipid trafficking
    • Awai K, Xu C, Tamot B, Benning C. 2006. A phosphatidic acid-binding protein of the chloroplast inner envelope membrane involved in lipid trafficking. Proc. Natl. Acad. Sci. USA 103:10817-22
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10817-10822
    • Awai, K.1    Xu, C.2    Tamot, B.3    Benning, C.4
  • 120
    • 37249092894 scopus 로고    scopus 로고
    • A small ATPase protein of Arabidopsis, TGD3, involved in chloroplast lipid import
    • Lu B, Xu C, Awai K, Jones AD, Benning C. 2007. A small ATPase protein of Arabidopsis, TGD3, involved in chloroplast lipid import. J. Biol. Chem. 282:35945-53
    • (2007) J. Biol. Chem , vol.282 , pp. 35945-35953
    • Lu, B.1    Xu, C.2    Awai, K.3    Jones, A.D.4    Benning, C.5
  • 121
    • 57749094124 scopus 로고    scopus 로고
    • Lipid trafficking between the endoplasmic reticulum and the plastid and Arabidopsis requires the extraplastidic TGD4 protein
    • Xu C, Fan J, Cornish A, Benning C. 2008. Lipid trafficking between the endoplasmic reticulum and the plastid and Arabidopsis requires the extraplastidic TGD4 protein. Plant Cell 20:2190-204
    • (2008) Plant Cell , vol.20 , pp. 2190-2204
    • Xu, C.1    Fan, J.2    Cornish, A.3    Benning, C.4
  • 122
    • 0347611095 scopus 로고    scopus 로고
    • Molecular machinery for nonvesicular trafficking of ceramide
    • Hanada K, Kumagai K, Yasuda S, Miura Y, Kawano M, et al. 2003. Molecular machinery for nonvesicular trafficking of ceramide. Nature 426:803-9
    • (2003) Nature , vol.426 , pp. 803-809
    • Hanada, K.1    Kumagai, K.2    Yasuda, S.3    Miura, Y.4    Kawano, M.5
  • 123
  • 124
    • 28044469878 scopus 로고    scopus 로고
    • Phosphatidylserine decarboxylases as genetic and biochemical tools for studying phospholipid traffic
    • Choi JY, Wu WI, Voelker DR. 2005. Phosphatidylserine decarboxylases as genetic and biochemical tools for studying phospholipid traffic. Anal. Biochem. 347:165-75
    • (2005) Anal. Biochem , vol.347 , pp. 165-175
    • Choi, J.Y.1    Wu, W.I.2    Voelker, D.R.3
  • 125
    • 0027973135 scopus 로고
    • A unique mitochondria- associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins
    • Rusinol AE, Cui Z, Chen MH, Vance JE. 1994. A unique mitochondria- associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J. Biol. Chem. 269:27494-502
    • (1994) J. Biol. Chem , vol.269 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 126
    • 0034604341 scopus 로고    scopus 로고
    • Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCF(Met30)-mediated inactivation of the transcription factor Met4
    • Kaiser P, Flick K, Wittenberg C, Reed SI. 2000. Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCF(Met30)-mediated inactivation of the transcription factor Met4. Cell 102:303-14
    • (2000) Cell , vol.102 , pp. 303-314
    • Kaiser, P.1    Flick, K.2    Wittenberg, C.3    Reed, S.I.4
  • 127
    • 0032557556 scopus 로고    scopus 로고
    • A genetic screen for aminophospholipid transport mutants identifies the phosphatidylinositol 4-kinase, STT4p, as an essential component in phosphatidylserine metabolism
    • Trotter PJ, Wu WI, Pedretti J, Yates R, Voelker DR. 1998. A genetic screen for aminophospholipid transport mutants identifies the phosphatidylinositol 4-kinase, STT4p, as an essential component in phosphatidylserine metabolism. J. Biol. Chem. 273:13189-96
    • (1998) J. Biol. Chem , vol.273 , pp. 13189-13196
    • Trotter, P.J.1    Wu, W.I.2    Pedretti, J.3    Yates, R.4    Voelker, D.R.5
  • 128
    • 0034640517 scopus 로고    scopus 로고
    • A new gene involved in the transport-dependent metabolism of phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene encoding the phosphatidylinositol/ phosphatidylcholine transfer protein, SEC14
    • Wu WI, Routt S, Bankaitis VA, Voelker DR. 2000. A new gene involved in the transport-dependent metabolism of phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene encoding the phosphatidylinositol/ phosphatidylcholine transfer protein, SEC14. J. Biol. Chem. 275:14446-56
    • (2000) J. Biol. Chem , vol.275 , pp. 14446-14456
    • Wu, W.I.1    Routt, S.2    Bankaitis, V.A.3    Voelker, D.R.4
  • 129
    • 0037072811 scopus 로고    scopus 로고
    • The C2 domain of phosphatidylserine decarboxylase 2 is not required for catalysis but is essential for in vivo function
    • Kitamura H, Wu WI, Voelker DR. 2002. The C2 domain of phosphatidylserine decarboxylase 2 is not required for catalysis but is essential for in vivo function. J. Biol. Chem. 277:33720-26
    • (2002) J. Biol. Chem , vol.277 , pp. 33720-33726
    • Kitamura, H.1    Wu, W.I.2    Voelker, D.R.3
  • 130
    • 0036001334 scopus 로고    scopus 로고
    • Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade
    • Audhya A, Emr SD. 2002. Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade. Dev. Cell 2:593-605
    • (2002) Dev. Cell , vol.2 , pp. 593-605
    • Audhya, A.1    Emr, S.D.2
  • 131
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin AC, Bosche M, Krause R, Grandi P, Marzioch M, et al. 2002. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415:141-47
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5
  • 132
    • 0000942202 scopus 로고    scopus 로고
    • PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs
    • Van Den Hazel HB, Pichler H, do Valle Matta MA, Leitner E, Goffeau A, Daum G. 1999. PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs. J. Biol. Chem. 274:1934-41
    • (1999) J. Biol. Chem , vol.274 , pp. 1934-1941
    • Van1    Den Hazel, H.B.2    Pichler, H.3    do Valle4    Matta, M.A.5    Leitner, E.6    Goffeau, A.7    Daum, G.8
  • 133
    • 0033179969 scopus 로고    scopus 로고
    • Yeast Sec14p deficient in phosphatidylinositol transfer activity is functional in vivo
    • Phillips SE, Sha B, Topalof L, Xie Z, Alb JG, et al. 1999. Yeast Sec14p deficient in phosphatidylinositol transfer activity is functional in vivo. Mol. Cell 4:187-97
    • (1999) Mol. Cell , vol.4 , pp. 187-197
    • Phillips, S.E.1    Sha, B.2    Topalof, L.3    Xie, Z.4    Alb, J.G.5
  • 134
    • 0028924622 scopus 로고
    • Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele
    • Trotter PJ, Pedretti J, Yates R, Voelker DR. 1995. Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele. J. Biol. Chem. 270:6071-80
    • (1995) J. Biol. Chem , vol.270 , pp. 6071-6080
    • Trotter, P.J.1    Pedretti, J.2    Yates, R.3    Voelker, D.R.4
  • 135
    • 2342637722 scopus 로고    scopus 로고
    • Oxysterol binding proteins: In more than one place at one time?
    • Olkkonen VM, Levine TP. 2004. Oxysterol binding proteins: in more than one place at one time? Biochem. Cell Biol. 82:87-98
    • (2004) Biochem. Cell Biol , vol.82 , pp. 87-98
    • Olkkonen, V.M.1    Levine, T.P.2
  • 136
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Im YJ, Raychaudhuri S, Prinz WA, Hurley JH. 2005. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437:154-58
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 137
    • 0036792481 scopus 로고    scopus 로고
    • High-flux mitochondrial cholesterol trafficking, a specialized function of the adrenal cortex
    • Jefcoate C. 2002. High-flux mitochondrial cholesterol trafficking, a specialized function of the adrenal cortex. J. Clin. Investig. 110:881-90
    • (2002) J. Clin. Investig , vol.110 , pp. 881-890
    • Jefcoate, C.1
  • 138
    • 0034899563 scopus 로고    scopus 로고
    • Tracking the role of a star in the sky of the new millennium
    • Stocco DM. 2001. Tracking the role of a star in the sky of the new millennium. Mol. Endocrinol. 15:1245-54
    • (2001) Mol. Endocrinol , vol.15 , pp. 1245-1254
    • Stocco, D.M.1
  • 139
    • 33845977384 scopus 로고    scopus 로고
    • Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis
    • Liu J, Rone MB, Papadopoulos V. 2006. Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis. J. Biol. Chem. 281:38879-93
    • (2006) J. Biol. Chem , vol.281 , pp. 38879-38893
    • Liu, J.1    Rone, M.B.2    Papadopoulos, V.3
  • 140
    • 0031453141 scopus 로고    scopus 로고
    • Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity
    • Arakane F, King SR, Du Y, Kallen CB, Walsh LP, et al. 1997. Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity. J. Biol. Chem. 272:32656-62
    • (1997) J. Biol. Chem , vol.272 , pp. 32656-32662
    • Arakane, F.1    King2    SR, D.Y.3    Kallen, C.B.4    Walsh, L.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.