메뉴 건너뛰기




Volumn 510, Issue 7503, 2014, Pages 48-57

Lipid landscapes and pipelines in membrane homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

LIPID;

EID: 84901935763     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13474     Document Type: Review
Times cited : (668)

References (96)
  • 1
    • 22144478635 scopus 로고    scopus 로고
    • The emerging field of lipidomics
    • Wenk, M. R. The emerging field of lipidomics. Nature Rev. Drug Discov. 4, 594-610 (2005).
    • (2005) Nature Rev. Drug Discov. , vol.4 , pp. 594-610
    • Wenk, M.R.1
  • 2
    • 77954956306 scopus 로고    scopus 로고
    • Lipidomics: Coming to grips with lipid diversity
    • Shevchenko, A. & Simons, K. Lipidomics: coming to grips with lipid diversity. Nature Rev. Mol. Cell Biol. 11, 593-598 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 593-598
    • Shevchenko, A.1    Simons, K.2
  • 3
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe, H. J., Stevens, T. J. & Munro, S. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 142, 158-169 (2010).
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 4
    • 84869040414 scopus 로고    scopus 로고
    • Curvature lipid packing, and electrostatics of membrane organelles: Defining cellular territories in determining specificity
    • Bigay, J. & Antonny, B. Curvature, lipid packing, and electrostatics of membrane organelles: defining cellular territories in determining specificity. Dev. Cell 23, 886-895 (2012).
    • (2012) Dev. Cell , vol.23 , pp. 886-895
    • Bigay, J.1    Antonny, B.2
  • 5
    • 84883453530 scopus 로고    scopus 로고
    • Insights into the mechanisms of sterol transport between organelles
    • Mesmin, B., Antonny, B. & Drin, G. Insights into the mechanisms of sterol transport between organelles. Cell. Mol. Life Sci. 70, 3405-3421 (2013).
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 3405-3421
    • Mesmin, B.1    Antonny, B.2    Drin, G.3
  • 6
    • 84878131033 scopus 로고    scopus 로고
    • Checks and balances in membrane phospholipid class and acyl chain homeostasis, the yeast perspective
    • de Kroon, A. I. P. M., Rijken, P. J. & De Smet, C. H. Checks and balances in membrane phospholipid class and acyl chain homeostasis, the yeast perspective. Prog. Lipid Res. 52, 374-394 (2013).
    • (2013) Prog. Lipid Res. , vol.52 , pp. 374-394
    • De Kroon, A.I.P.M.1    Rijken, P.J.2    De Smet, C.H.3
  • 7
    • 0032578027 scopus 로고    scopus 로고
    • Phases and phase transitions of the phosphatidylcholines
    • Koynova, R. & Caffrey, M. Phases and phase transitions of the phosphatidylcholines. Biochim. Biophys. Acta 1376, 91-145 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 91-145
    • Koynova, R.1    Caffrey, M.2
  • 8
    • 36849039435 scopus 로고    scopus 로고
    • Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes
    • Marsh, D. Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes. Biophys. J. 93, 3884-3899 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 3884-3899
    • Marsh, D.1
  • 10
    • 77950561967 scopus 로고    scopus 로고
    • Pivotal advance: Phospholipids determine net membrane surface charge resulting in differential localization of active Rac1 and Rac2
    • Magalhaes, M. A. O. & Glogauer, M. Pivotal advance: phospholipids determine net membrane surface charge resulting in differential localization of active Rac1 and Rac2. J. Leukoc. Biol. 87, 545-555 (2010).
    • (2010) J. Leukoc. Biol. , vol.87 , pp. 545-555
    • Magalhaes, M.A.O.1    Glogauer, M.2
  • 11
    • 78349297851 scopus 로고    scopus 로고
    • Imaging signal transduction during phagocytosis: Phospholipids, surface charge, and electrostatic interactions
    • Grinstein, S. Imaging signal transduction during phagocytosis: phospholipids, surface charge, and electrostatic interactions. Am. J. Physiol. Cell Physiol. 299, C876-C881 (2010).
    • (2010) Am. J. Physiol. Cell Physiol. , vol.299
    • Grinstein, S.1
  • 13
    • 84878412799 scopus 로고    scopus 로고
    • Biological functions of sphingomyelins
    • Slotte, J. P. Biological functions of sphingomyelins. Prog. Lipid Res. 52, 424-437 (2013).
    • (2013) Prog. Lipid Res. , vol.52 , pp. 424-437
    • Slotte, J.P.1
  • 14
    • 0028906120 scopus 로고
    • Phases and phase transitions of the sphingolipids
    • Koynova, R. & Caffrey, M. Phases and phase transitions of the sphingolipids. Biochim. Biophys. Acta 1255, 213-236 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1255 , pp. 213-236
    • Koynova, R.1    Caffrey, M.2
  • 16
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown, D. A. & London, E. Structure and origin of ordered lipid domains in biological membranes. J. Membr. Biol. 164, 103-114 (1998).
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 17
    • 31944436780 scopus 로고    scopus 로고
    • Depletion of phosphatidylcholine in yeast induces shortening and increased saturation of the lipid acyl chains: Evidence for regulation of intrinsic membrane curvature in a eukaryote
    • Boumann, H. A. et al. Depletion of phosphatidylcholine in yeast induces shortening and increased saturation of the lipid acyl chains: evidence for regulation of intrinsic membrane curvature in a eukaryote. Mol. Biol. Cell 17, 1006-1017 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1006-1017
    • Boumann, H.A.1
  • 18
    • 0024268457 scopus 로고
    • Disruption of the CHO1 gene encoding phosphatidylserine synthase in Saccharomyces cerevisiae
    • Hikiji, T., Miura, K., Kiyono, K., Shibuya, I. & Ohta, A. Disruption of the CHO1 gene encoding phosphatidylserine synthase in Saccharomyces cerevisiae. J. Biochem. 104, 894-900 (1988).
    • (1988) J. Biochem. , vol.104 , pp. 894-900
    • Hikiji, T.1    Miura, K.2    Kiyono, K.3    Shibuya, I.4    Ohta, A.5
  • 19
    • 0027404090 scopus 로고
    • Mutant strains of Saccharomyces cerevisiae lacking sphingolipids synthesize novel inositol glycerophospholipids that mimic sphingolipid structures
    • Lester, R. L., Wells, G. B., Oxford, G. & Dickson, R. C. Mutant strains of Saccharomyces cerevisiae lacking sphingolipids synthesize novel inositol glycerophospholipids that mimic sphingolipid structures. J. Biol. Chem. 268, 845-856 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 845-856
    • Lester, R.L.1    Wells, G.B.2    Oxford, G.3    Dickson, R.C.4
  • 20
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park, E. & Rapoport, T. A. Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu. Rev. Biophys. 41, 21-40 (2012).
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 21
    • 56449110891 scopus 로고    scopus 로고
    • Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: A delicate balance
    • Radhakrishnan, A., Goldstein, J. L., McDonald, J. G. & Brown, M. S. Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance. Cell Metab. 8, 512-521 (2008).
    • (2008) Cell Metab. , vol.8 , pp. 512-521
    • Radhakrishnan, A.1    Goldstein, J.L.2    McDonald, J.G.3    Brown, M.S.4
  • 22
    • 0034789931 scopus 로고    scopus 로고
    • The organizing potential of sphingolipids in intracellular membrane transport
    • Holthuis, J. C., Pomorski, T., Raggers, R. J., Sprong, H. & Van Meer, G. The organizing potential of sphingolipids in intracellular membrane transport. Physiol. Rev. 81, 1689-1723 (2001).
    • (2001) Physiol. Rev. , vol.81 , pp. 1689-1723
    • Holthuis, J.C.1    Pomorski, T.2    Raggers, R.J.3    Sprong, H.4    Van Meer, G.5
  • 23
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter, R. et al. Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J. Cell Biol. 146, 741-754 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 741-754
    • Schneiter, R.1
  • 24
    • 0023839340 scopus 로고
    • Depletion of plasma-membrane sphingomyelin rapidly alters the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts
    • Slotte, J. P. & Bierman, E. L. Depletion of plasma-membrane sphingomyelin rapidly alters the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts. Biochem. J. 250, 653-658 (1988).
    • (1988) Biochem. J. , vol.250 , pp. 653-658
    • Slotte, J.P.1    Bierman, E.L.2
  • 25
    • 0034735575 scopus 로고    scopus 로고
    • Evidence for segregation of sphingomyelin and cholesterol during formation of COPI-coated vesicles
    • Brügger, B. et al. Evidence for segregation of sphingomyelin and cholesterol during formation of COPI-coated vesicles. J. Cell Biol. 151, 507-518 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 507-518
    • Brügger, B.1
  • 26
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro, S. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J. 14, 4695-4704 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 27
    • 84890218898 scopus 로고    scopus 로고
    • Short transmembrane domains with high-volume exoplasmic halves determine retention of Type II membrane proteins in the Golgi complex
    • Quiroga, R., Trenchi, A., González Montoro, A., Valdez Taubas, J. & Maccioni, H. J. F. Short transmembrane domains with high-volume exoplasmic halves determine retention of Type II membrane proteins in the Golgi complex. J. Cell Sci. 126, 5344-5349 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 5344-5349
    • Quiroga, R.1    Trenchi, A.2    González Montoro, A.3    Valdez Taubas, J.4    MacCioni, H.J.F.5
  • 28
    • 80053632190 scopus 로고    scopus 로고
    • Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching
    • Kaiser, H.-J. et al. Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching. Proc. Natl Acad. Sci. USA 108, 16628-16633 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 16628-16633
    • Kaiser, H.-J.1
  • 29
    • 79961113678 scopus 로고    scopus 로고
    • High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine
    • Fairn, G. D. et al. High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine. J. Cell Biol. 194, 257-275 (2011).
    • (2011) J. Cell Biol. , vol.194 , pp. 257-275
    • Fairn, G.D.1
  • 30
    • 73449119238 scopus 로고    scopus 로고
    • Flipping lipids: Why an' what's the reason for ACS Chem
    • Sanyal, S. & Menon, A. K. Flipping lipids: why an' what's the reason for ACS Chem. Biol. 4, 895-909 (2009).
    • (2009) Biol. , vol.4 , pp. 895-909
    • Sanyal, S.1    Menon, A.K.2
  • 31
    • 34147152663 scopus 로고    scopus 로고
    • Lipidomics reveals that adiposomes store ether lipids and mediate phospholipid traffic
    • Bartz, R. et al. Lipidomics reveals that adiposomes store ether lipids and mediate phospholipid traffic. J. Lipid Res. 48, 837-847 (2007).
    • (2007) J. Lipid Res. , vol.48 , pp. 837-847
    • Bartz, R.1
  • 32
    • 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, T. R. Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function. Proc. Natl Acad. Sci. USA 101, 10614-10619 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10614-10619
    • Natarajan, P.1    Wang, J.2    Hua, Z.3    Graham, T.R.4
  • 33
    • 33745413294 scopus 로고    scopus 로고
    • 4 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, J. C. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17, 1632-1642 (2006).
    • (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
  • 34
    • 80755129133 scopus 로고    scopus 로고
    • A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes
    • Kim, Y. J., Guzman-Hernandez, M. L. & Balla, T. A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes. Dev. Cell 21, 813-824 (2011).
    • (2011) Dev. Cell , vol.21 , pp. 813-824
    • Kim, Y.J.1    Guzman-Hernandez, M.L.2    Balla, T.3
  • 35
    • 84873375687 scopus 로고    scopus 로고
    • Amphipathic lipid packing sensor motifs: Probing bilayer defects with hydrophobic residues
    • Vanni, S. et al. Amphipathic lipid packing sensor motifs: probing bilayer defects with hydrophobic residues. Biophys. J. 104, 575-584 (2013).
    • (2013) Biophys. J. , vol.104 , pp. 575-584
    • Vanni, S.1
  • 36
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • Levine, T. Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol. 14, 483-490 (2004).
    • (2004) Trends Cell Biol. , vol.14 , pp. 483-490
    • Levine, T.1
  • 37
    • 77957134067 scopus 로고    scopus 로고
    • Non-vesicular lipid transport by lipid-transfer proteins and beyond
    • Lev, S. Non-vesicular lipid transport by lipid-transfer proteins and beyond. Nature Rev. Mol. Cell Biol. 11, 739-750 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 739-750
    • Lev, S.1
  • 38
    • 44949214679 scopus 로고    scopus 로고
    • Differential regulation of the endoplasmic reticulum stress response in pancreatic β-cells exposed to long-chain saturated and monounsaturated fatty acids
    • Diakogiannaki, E., Welters, H. J. & Morgan, N. G. Differential regulation of the endoplasmic reticulum stress response in pancreatic β-cells exposed to long-chain saturated and monounsaturated fatty acids. J. Endocrinol. 197, 553-563 (2008).
    • (2008) J. Endocrinol. , vol.197 , pp. 553-563
    • Diakogiannaki, E.1    Welters, H.J.2    Morgan, N.G.3
  • 39
    • 79751486464 scopus 로고    scopus 로고
    • Modulation of lipid-induced ER stress by fatty acid shape
    • Deguil, J. et al. Modulation of lipid-induced ER stress by fatty acid shape. Traffic 12, 349-362 (2011).
    • (2011) Traffic , vol.12 , pp. 349-362
    • Deguil, J.1
  • 41
    • 84895814979 scopus 로고    scopus 로고
    • A lipid-mediated conformational switch modulates the thermosensing activity of DesK
    • Inda, M. E. et al. A lipid-mediated conformational switch modulates the thermosensing activity of DesK. Proc. Natl Acad. Sci. USA 111, 3579-3584 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 3579-3584
    • Inda, M.E.1
  • 42
    • 63449128473 scopus 로고    scopus 로고
    • Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum
    • Jonikas, M. C. et al. Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323, 1693-1697 (2009).
    • (2009) Science , vol.323 , pp. 1693-1697
    • Jonikas, M.C.1
  • 43
    • 84882669269 scopus 로고    scopus 로고
    • A lipid E-MAP identifies Ubx2 as a critical regulator of lipid saturation and lipid bilayer stress
    • Surma, M. A. et al. A lipid E-MAP identifies Ubx2 as a critical regulator of lipid saturation and lipid bilayer stress. Mol. Cell 51, 519-530 (2013).
    • (2013) Mol. Cell , vol.51 , pp. 519-530
    • Surma, M.A.1
  • 44
    • 73349106233 scopus 로고    scopus 로고
    • Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response
    • Schuck, S., Prinz, W. A., Thorn, K. S., Voss, C. & Walter, P. Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J. Cell Biol. 187, 525-536 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 525-536
    • Schuck, S.1    Prinz, W.A.2    Thorn, K.S.3    Voss, C.4    Walter, P.5
  • 45
    • 80052825784 scopus 로고    scopus 로고
    • Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways
    • Promlek, T. et al. Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways. Mol. Biol. Cell 22, 3520-3532 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3520-3532
    • Promlek, T.1
  • 46
    • 84875242776 scopus 로고    scopus 로고
    • Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains
    • Volmer, R., van der Ploeg, K. & Ron, D. Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains. Proc. Natl Acad. Sci. USA 110, 4628-4633 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 4628-4633
    • Volmer, R.1    Van Der Ploeg, K.2    Ron, D.3
  • 47
    • 0035834729 scopus 로고    scopus 로고
    • Inhibition of protein translocation across the endoplasmic reticulum membrane by sterols
    • Nilsson, I., Ohvo-Rekilä, H., Slotte, J. P., Johnson, A. E. & von Heijne, G. Inhibition of protein translocation across the endoplasmic reticulum membrane by sterols. J. Biol. Chem. 276, 41748-41754 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 41748-41754
    • Nilsson, I.1    Ohvo-Rekilä, H.2    Slotte, J.P.3    Johnson, A.E.4    Von Heijne, G.5
  • 48
    • 84867474549 scopus 로고    scopus 로고
    • Ergosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes
    • Krumpe, K. et al. Ergosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes. Mol. Biol. Cell 23, 3927-3935 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3927-3935
    • Krumpe, K.1
  • 49
    • 81055140116 scopus 로고    scopus 로고
    • A conserved SREBP-1/phosphatidylcholine feedback circuit regulates lipogenesis in metazoans
    • Walker, A. K. et al. A conserved SREBP-1/phosphatidylcholine feedback circuit regulates lipogenesis in metazoans. Cell 147, 840-852 (2011).
    • (2011) Cell , vol.147 , pp. 840-852
    • Walker, A.K.1
  • 50
    • 84892648364 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of CTP:phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidylcholine synthesis, by its membrane-binding amphipathic helix
    • Lee, J., Taneva, S. G., Holland, B. W., Tieleman, D. P. & Cornell, R. B. Structural basis for autoinhibition of CTP:phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidylcholine synthesis, by its membrane-binding amphipathic helix. J. Biol. Chem. 289, 1742-1755 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 1742-1755
    • Lee, J.1    Taneva, S.G.2    Holland, B.W.3    Tieleman, D.P.4    Cornell, R.B.5
  • 51
    • 0034255144 scopus 로고    scopus 로고
    • Modulation of CTP: Phosphocholine cytidylyltransferase by membrane curvature elastic stress
    • Attard, G. S., Templer, R. H., Smith, W. S., Hunt, A. N. & Jackowski, S. Modulation of CTP:phosphocholine cytidylyltransferase by membrane curvature elastic stress. Proc. Natl Acad. Sci. USA 97, 9032-9036 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9032-9036
    • Attard, G.S.1    Templer, R.H.2    Smith, W.S.3    Hunt, A.N.4    Jackowski, S.5
  • 52
    • 80053927108 scopus 로고    scopus 로고
    • Phosphatidylcholine synthesis for lipid droplet expansion is mediated by localized activation of CTP:phosphocholine cytidylyltransferase
    • Krahmer, N. et al. Phosphatidylcholine synthesis for lipid droplet expansion is mediated by localized activation of CTP:phosphocholine cytidylyltransferase. Cell Metab. 14, 504-515 (2011).
    • (2011) Cell Metab. , vol.14 , pp. 504-515
    • Krahmer, N.1
  • 53
    • 84887957821 scopus 로고    scopus 로고
    • A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP
    • Mesmin, B. et al. A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP. Cell 155, 830-843 (2013).
    • (2013) Cell , vol.155 , pp. 830-843
    • Mesmin, B.1
  • 55
    • 0025142335 scopus 로고
    • Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane
    • Urbani, L. & Simoni, R. D. Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane. J. Biol. Chem. 265, 1919-1923 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 1919-1923
    • Urbani, L.1    Simoni, R.D.2
  • 56
    • 17144403817 scopus 로고    scopus 로고
    • Transport of newly synthesized sterol to the sterol-enriched plasma membrane occurs via nonvesicular equilibration
    • Baumann, N. A. et al. Transport of newly synthesized sterol to the sterol-enriched plasma membrane occurs via nonvesicular equilibration. Biochemistry 44, 5816-5826 (2005).
    • (2005) Biochemistry , vol.44 , pp. 5816-5826
    • Baumann, N.A.1
  • 57
    • 0022416616 scopus 로고
    • Intracellular transport of phosphatidylcholine to the plasma membrane
    • Kaplan, M. R. & Simoni, R. D. Intracellular transport of phosphatidylcholine to the plasma membrane. J. Cell Biol. 101, 441-445 (1985).
    • (1985) J. Cell Biol. , vol.101 , pp. 441-445
    • Kaplan, M.R.1    Simoni, R.D.2
  • 58
    • 0021099854 scopus 로고
    • Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane
    • Sleight, R. G. & Pagano, R. E. Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane. J. Biol. Chem. 258, 9050-9058 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 9050-9058
    • Sleight, R.G.1    Pagano, R.E.2
  • 59
    • 0034682501 scopus 로고    scopus 로고
    • Dissecting the role of the golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface
    • Heino, S. et al. Dissecting the role of the golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface. Proc. Natl Acad. Sci. USA 97, 8375-8380 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8375-8380
    • Heino, S.1
  • 60
    • 0347611095 scopus 로고    scopus 로고
    • Molecular machinery for non-vesicular trafficking of ceramide
    • Hanada, K. et al. Molecular machinery for non-vesicular trafficking of ceramide. Nature 426, 803-809 (2003).
    • (2003) Nature , vol.426 , pp. 803-809
    • Hanada, K.1
  • 61
    • 0024550057 scopus 로고
    • Lipid transport during mitosis. Alternative pathways for delivery of newly synthesized lipids to the cell surface
    • Kobayashi, T. & Pagano, R. E. Lipid transport during mitosis. Alternative pathways for delivery of newly synthesized lipids to the cell surface. J. Biol. Chem. 264, 5966-5973 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 5966-5973
    • Kobayashi, T.1    Pagano, R.E.2
  • 62
    • 84884210112 scopus 로고    scopus 로고
    • Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins
    • Maeda, K. et al. Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins. Nature 501, 257-261 (2013).
    • (2013) Nature , vol.501 , pp. 257-261
    • Maeda, K.1
  • 63
    • 13644269281 scopus 로고    scopus 로고
    • Multiple lipid transport pathways to the plasma membrane in yeast
    • Schnabl, M., Daum, G. & Pichler, H. Multiple lipid transport pathways to the plasma membrane in yeast. Biochim. Biophys. Acta 1687, 130-140 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1687 , pp. 130-140
    • Schnabl, M.1    Daum, G.2    Pichler, H.3
  • 64
    • 35348991132 scopus 로고    scopus 로고
    • Pre-and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis
    • Halter, D. et al. Pre-and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis. J. Cell Biol. 179, 101-115 (2007).
    • (2007) J. Cell Biol. , vol.179 , pp. 101-115
    • Halter, D.1
  • 65
    • 84883742330 scopus 로고    scopus 로고
    • Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi
    • D'Angelo, G. et al. Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi. Nature 501, 116-120 (2013).
    • (2013) Nature , vol.501 , pp. 116-120
    • D'Angelo, G.1
  • 66
    • 0027769775 scopus 로고
    • Spontaneous interbilayer transfer of phospholipids: Dependence on acyl chain composition
    • Silvius, J. R. & Leventis, R. Spontaneous interbilayer transfer of phospholipids: dependence on acyl chain composition. Biochemistry 32, 13318-13326 (1993).
    • (1993) Biochemistry , vol.32 , pp. 13318-13326
    • Silvius, J.R.1    Leventis, R.2
  • 67
    • 37349024764 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of the association of dehydroergosterol with lipid bilayer membranes
    • Estronca, L. M. B. B., Moreno, M. J. & Vaz, W. L. C. Kinetics and thermodynamics of the association of dehydroergosterol with lipid bilayer membranes. Biophys. J. 93, 4244-4253 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 4244-4253
    • Estronca, L.M.B.B.1    Moreno, M.J.2    Vaz, W.L.C.3
  • 68
    • 0025766081 scopus 로고
    • Phospholipid transfer proteins
    • Wirtz, K. W. Phospholipid transfer proteins. Annu. Rev. Biochem. 60, 73-99 (1991).
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 73-99
    • Wirtz, K.W.1
  • 69
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • Loewen, C. J. R., Roy, A. & Levine, T. P. A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP. EMBO J. 22, 2025-2035 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2025-2035
    • Loewen, C.J.R.1    Roy, A.2    Levine, T.P.3
  • 70
    • 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. 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, 30279-30288 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 30279-30288
    • Kawano, M.1    Kumagai, K.2    Nishijima, M.3    Hanada, K.4
  • 71
    • 84898657933 scopus 로고    scopus 로고
    • Phosphoregulation of the ceramide transport protein CERT at serine 315 in the interaction with VAMP-associated protein (VAP) for inter-organelle trafficking of ceramide in mammalian cells
    • Kumagai, K., Kawano-Kawada, M. & Hanada, K. Phosphoregulation of the ceramide transport protein CERT at serine 315 in the interaction with VAMP-associated protein (VAP) for inter-organelle trafficking of ceramide in mammalian cells. J. Biol. Chem. 289, 10748-10760 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 10748-10760
    • Kumagai, K.1    Kawano-Kawada, M.2    Hanada, K.3
  • 72
    • 33745759439 scopus 로고    scopus 로고
    • Intracellular sterol transport and distribution
    • Maxfield, F. R. & Menon, A. K. Intracellular sterol transport and distribution. Curr. Opin. Cell Biol. 18, 379-385 (2006).
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 379-385
    • Maxfield, F.R.1    Menon, A.K.2
  • 73
    • 65249161758 scopus 로고    scopus 로고
    • Oxysterol binding protein-related protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function
    • Ngo, M. & Ridgway, N. D. Oxysterol binding protein-related protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function. Mol. Biol. Cell 20, 1388-1399 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1388-1399
    • Ngo, M.1    Ridgway, N.D.2
  • 74
    • 77952314344 scopus 로고    scopus 로고
    • Oxysterol-binding proteins
    • Ridgway, N. D. Oxysterol-binding proteins. Subcell. Biochem. 51, 159-182 (2010).
    • (2010) Subcell. Biochem. , vol.51 , pp. 159-182
    • Ridgway, N.D.1
  • 75
    • 84855474121 scopus 로고    scopus 로고
    • Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers
    • de Saint-Jean, M. et al. Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers. J. Cell Biol. 195, 965-978 (2011).
    • (2011) J. Cell Biol. , vol.195 , pp. 965-978
    • De Saint-Jean, M.1
  • 76
    • 78650123509 scopus 로고    scopus 로고
    • Oxysterol binding protein-dependent activation of sphingomyelin synthesis in the golgi apparatus requires phosphatidylinositol 4-kinase IIα
    • Banerji, S. et al. Oxysterol binding protein-dependent activation of sphingomyelin synthesis in the golgi apparatus requires phosphatidylinositol 4-kinase IIα. Mol. Biol. Cell 21, 4141-4150 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4141-4150
    • Banerji, S.1
  • 77
    • 0035842889 scopus 로고    scopus 로고
    • Vesicular and nonvesicular transport of ceramide from ER to the Golgi apparatus in yeast
    • Funato, K. & Riezman, H. Vesicular and nonvesicular transport of ceramide from ER to the Golgi apparatus in yeast. J. Cell Biol. 155, 949-959 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 949-959
    • Funato, K.1    Riezman, H.2
  • 78
    • 84874713274 scopus 로고    scopus 로고
    • Sphingolipid homeostasis in the endoplasmic reticulum and beyond
    • Breslow, D. K. Sphingolipid homeostasis in the endoplasmic reticulum and beyond. Cold Spring Harb. Perspect. Biol. 5, a013326 (2013).
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5
    • Breslow, D.K.1
  • 79
    • 77649121162 scopus 로고    scopus 로고
    • Orm family proteins mediate sphingolipid homeostasis
    • Breslow, D. K. et al. Orm family proteins mediate sphingolipid homeostasis. Nature 463, 1048-1053 (2010).
    • (2010) Nature , vol.463 , pp. 1048-1053
    • Breslow, D.K.1
  • 80
    • 77950541324 scopus 로고    scopus 로고
    • Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control
    • Han, S., Lone, M. A., Schneiter, R. & Chang, A. Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control. Proc. Natl Acad. Sci. USA 107, 5851-5856 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 5851-5856
    • Han, S.1    Lone, M.A.2    Schneiter, R.3    Chang, A.4
  • 81
    • 82755163564 scopus 로고    scopus 로고
    • Protein kinase Ypk1 phosphorylates regulatory proteins Orm1 and Orm2 to control sphingolipid homeostasis in Saccharomyces cerevisiae
    • Roelants, F. M., Breslow, D. K., Muir, A., Weissman, J. S. & Thorner, J. Protein kinase Ypk1 phosphorylates regulatory proteins Orm1 and Orm2 to control sphingolipid homeostasis in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 108, 19222-19227 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 19222-19227
    • Roelants, F.M.1    Breslow, D.K.2    Muir, A.3    Weissman, J.S.4    Thorner, J.5
  • 82
    • 44949237144 scopus 로고    scopus 로고
    • Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry
    • Nakano, K., Yamamoto, T., Kishimoto, T., Noji, T. & Tanaka, K. Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol. Biol. Cell 19, 1783-1797 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1783-1797
    • Nakano, K.1    Yamamoto, T.2    Kishimoto, T.3    Noji, T.4    Tanaka, K.5
  • 84
    • 20444473800 scopus 로고    scopus 로고
    • Mechanisms of disease: Pathogenesis of nonalcoholic fatty liver disease
    • Sanyal, A. J. Mechanisms of disease: pathogenesis of nonalcoholic fatty liver disease. Nature Clin. Pract. Gastroenterol. Hepatol. 2, 46-53 (2005).
    • (2005) Nature Clin. Pract. Gastroenterol. Hepatol. , vol.2 , pp. 46-53
    • Sanyal, A.J.1
  • 86
    • 84887324215 scopus 로고    scopus 로고
    • Lipotoxicity in the liver
    • Zámbó, V. et al. Lipotoxicity in the liver. World J. Hepatol. 5, 550-557 (2013).
    • (2013) World J. Hepatol. , vol.5 , pp. 550-557
    • Zámbó, V.1
  • 87
    • 4344578601 scopus 로고    scopus 로고
    • Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids: Implications for depletion of endoplasmic reticulum calcium stores and apoptosis in cholesterol-loaded macrophages
    • Li, Y. et al. Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids: implications for depletion of endoplasmic reticulum calcium stores and apoptosis in cholesterol-loaded macrophages. J. Biol. Chem. 279, 37030-37039 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 37030-37039
    • Li, Y.1
  • 88
    • 79957605136 scopus 로고    scopus 로고
    • Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity
    • Fu, S. et al. Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity. Nature 473, 528-531 (2011).
    • (2011) Nature , vol.473 , pp. 528-531
    • Fu, S.1
  • 89
    • 84882577354 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress leads to lipid accumulation through upregulation of SREBP-1c in normal hepatic and hepatoma cells
    • Fang, D.-L. et al. Endoplasmic reticulum stress leads to lipid accumulation through upregulation of SREBP-1c in normal hepatic and hepatoma cells. Mol. Cell. Biochem. 381, 127-137 (2013).
    • (2013) Mol. Cell. Biochem. , vol.381 , pp. 127-137
    • Fang, D.-L.1
  • 90
    • 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, C. C. et al. Atp8b1 deficiency in mice reduces resistance of the canalicular membrane to hydrophobic bile salts and impairs bile salt transport. Hepatology 44, 195-204 (2006).
    • (2006) Hepatology , vol.44 , pp. 195-204
    • Paulusma, C.C.1
  • 91
    • 0141706384 scopus 로고    scopus 로고
    • Biliary diversion for progressive familial intrahepatic cholestasis: Improved liver morphology and bile acid profile
    • Kurbegov, A. C. et al. Biliary diversion for progressive familial intrahepatic cholestasis: improved liver morphology and bile acid profile. Gastroenterology 125, 1227-1234 (2003).
    • (2003) Gastroenterology , vol.125 , pp. 1227-1234
    • Kurbegov, A.C.1
  • 92
    • 65649087129 scopus 로고    scopus 로고
    • Activity of the bile salt export pump (ABCB11) is critically dependent on canalicular membrane cholesterol content
    • Paulusma, C. C., de Waart, D. R., Kunne, C., Mok, K. S. & Elferink, R. P. J. O. Activity of the bile salt export pump (ABCB11) is critically dependent on canalicular membrane cholesterol content. J. Biol. Chem. 284, 9947-9954 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 9947-9954
    • Paulusma, C.C.1    De Waart, D.R.2    Kunne, C.3    Mok, K.S.4    Elferink, R.P.J.O.5
  • 93
    • 84865660375 scopus 로고    scopus 로고
    • Thoughts on Sec14-like nanoreactors and phosphoinositide signaling
    • Bankaitis, V. A. et al. Thoughts on Sec14-like nanoreactors and phosphoinositide signaling. Adv. Biol. Regul. 52, 115-121 (2012).
    • (2012) Adv. Biol. Regul. , vol.52 , pp. 115-121
    • Bankaitis, V.A.1
  • 94
    • 84890558909 scopus 로고    scopus 로고
    • START ships lipids across interorganelle space
    • Alpy, F. & Tomasetto, C. START ships lipids across interorganelle space. Biochimie 96, 85-95 (2014).
    • (2014) Biochimie , vol.96 , pp. 85-95
    • Alpy, F.1    Tomasetto, C.2
  • 95
    • 80052630805 scopus 로고    scopus 로고
    • Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM
    • Georgiev, A. G. et al. Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM. Traffic 12, 1341-1355 (2011).
    • (2011) Traffic , vol.12 , pp. 1341-1355
    • Georgiev, A.G.1
  • 96
    • 44449129087 scopus 로고    scopus 로고
    • Protein phosphatase 2Cε is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes
    • Saito, S. et al. Protein phosphatase 2Cε 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, 6584-6593 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 6584-6593
    • Saito, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.