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Volumn 18, Issue 11, 2013, Pages 13666-13679

OSBP-related proteins: Liganding by glycerophospholipids opens new insight into their function

Author keywords

Cell signaling; Cholesterol; Lipid metabolism; LTP; ORP; OSBPL; Osh; Oxysterol; Phospholipid

Indexed keywords

GLYCEROPHOSPHOLIPID; OXYSTEROL BINDING PROTEIN; STEROID RECEPTOR;

EID: 84888599744     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules181113666     Document Type: Article
Times cited : (22)

References (73)
  • 4
    • 84862192727 scopus 로고    scopus 로고
    • Vesicle-mediated ER export of proteins and lipids
    • Gillon, A.D.; Latham, C.F.; Miller, E.A. Vesicle-mediated ER export of proteins and lipids. Biochim Biophys Acta 2012, 1821, 1040-1049.
    • (2012) Biochim Biophys Acta , vol.1821 , pp. 1040-1049
    • Gillon, A.D.1    Latham, C.F.2    Miller, E.A.3
  • 5
    • 3142516233 scopus 로고    scopus 로고
    • Membrane lipids and vesicular traffic
    • Van Meer, G.; Sprong, H. Membrane lipids and vesicular traffic. Curr. Opin. Cell. Biol. 2004, 16, 373-378.
    • (2004) Curr. Opin. Cell. Biol. , vol.16 , pp. 373-378
    • Van Meer, G.1    Sprong, H.2
  • 7
    • 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. Nat. Rev. Mol. Cell. Biol. 2010, 11, 739-750.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 739-750
    • Lev, S.1
  • 8
    • 80755153578 scopus 로고    scopus 로고
    • Staying in touch: The molecular era of organelle contact sites
    • Elbaz, Y.; Schuldiner, M. Staying in touch: The molecular era of organelle contact sites. Trends Biochem. Sci. 2011, 36, 616-623.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 616-623
    • Elbaz, Y.1    Schuldiner, M.2
  • 9
    • 33745755614 scopus 로고    scopus 로고
    • Inter-organelle membrane contact sites: Through a glass, darkly
    • Levine, T.; Loewen, C. Inter-organelle membrane contact sites: through a glass, darkly. Curr. Opin. Cell. Biol. 2006, 18, 371-378.
    • (2006) Curr. Opin. Cell. Biol. , vol.18 , pp. 371-378
    • Levine, T.1    Loewen, C.2
  • 10
    • 84883451938 scopus 로고    scopus 로고
    • ER-PM connections: Sites of information transfer and inter-organelle communication
    • Stefan, C.J.; Manford, A.G.; Emr, S.D. ER-PM connections: Sites of information transfer and inter-organelle communication. Curr. Opin. Cell. Biol. 2013, 25, 434-442.
    • (2013) Curr. Opin. Cell. Biol. , vol.25 , pp. 434-442
    • Stefan, C.J.1    Manford, A.G.2    Emr, S.D.3
  • 11
    • 79960739849 scopus 로고    scopus 로고
    • Lipid transfer and signaling at organelle contact sites: The tip of the iceberg
    • Toulmay, A.; Prinz, W.A. Lipid transfer and signaling at organelle contact sites: The tip of the iceberg. Curr. Opin. Cell. Biol. 2011, 23, 458-463.
    • (2011) Curr. Opin. Cell. Biol. , vol.23 , pp. 458-463
    • Toulmay, A.1    Prinz, W.A.2
  • 12
    • 77955053533 scopus 로고    scopus 로고
    • Cholesterol, the central lipid of mammalian cells
    • Maxfield, F.R.; van Meer, G. Cholesterol, the central lipid of mammalian cells. Curr. Opin. Cell. Biol. 2010, 22, 422-429.
    • (2010) Curr. Opin. Cell. Biol. , vol.22 , pp. 422-429
    • Maxfield, F.R.1    Van Meer, G.2
  • 13
    • 38549141572 scopus 로고    scopus 로고
    • Cellular cholesterol trafficking and compartmentalization
    • Ikonen, E. Cellular cholesterol trafficking and compartmentalization. Nat. Rev. Mol. Cell. Biol. 2008, 9, 125-138.
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 125-138
    • Ikonen, E.1
  • 15
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • Voelker, D.R. Bridging gaps in phospholipid transport. Trends Biochem Sci 2005, 30, 396-404.
    • (2005) Trends Biochem Sci , vol.30 , pp. 396-404
    • Voelker, D.R.1
  • 16
    • 67650747650 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of non-vesicular lipid traffic
    • Voelker, D.R. Genetic and biochemical analysis of non-vesicular lipid traffic. Annu. Rev. Biochem. 2009, 78, 827-856.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 827-856
    • Voelker, D.R.1
  • 17
    • 0036096897 scopus 로고    scopus 로고
    • Oxysterols: Friends, foes, or just fellow passengers? Arterioscler
    • Björkhem, I.; Diczfalusy, U. Oxysterols: Friends, foes, or just fellow passengers? Arterioscler. Thromb. Vasc. Biol. 2002, 22, 734-742.
    • (2002) Thromb. Vasc. Biol. , vol.22 , pp. 734-742
    • Björkhem, I.1    Diczfalusy, U.2
  • 18
    • 0034672672 scopus 로고    scopus 로고
    • Oxysterol biosynthetic enzymes
    • Russell, D.W. Oxysterol biosynthetic enzymes. Biochim. Biophys. Acta 2000, 1529, 126-135.
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 126-135
    • Russell, D.W.1
  • 19
    • 0032890337 scopus 로고    scopus 로고
    • Oxysterols and atherosclerosis
    • Brown, A.J.; Jessup, W. Oxysterols and atherosclerosis. Atherosclerosis 1999, 142, 1-28.
    • (1999) Atherosclerosis , vol.142 , pp. 1-28
    • Brown, A.J.1    Jessup, W.2
  • 21
    • 0028999147 scopus 로고
    • Movement of 25-hydroxycholesterol from the plasma membrane to the rough endoplasmic reticulum in cultured hepatoma cells
    • Lange, Y.; Ye, J.; Strebel, F. Movement of 25-hydroxycholesterol from the plasma membrane to the rough endoplasmic reticulum in cultured hepatoma cells. J. Lipid Res. 1995, 36, 1092-1097.
    • (1995) J. Lipid Res. , vol.36 , pp. 1092-1097
    • Lange, Y.1    Ye, J.2    Strebel, F.3
  • 22
    • 33646864114 scopus 로고    scopus 로고
    • Membrane and protein interactions of oxysterols
    • Massey, J.B. Membrane and protein interactions of oxysterols. Curr. Opin. Lipidol. 2006, 17, 296-301.
    • (2006) Curr. Opin. Lipidol. , vol.17 , pp. 296-301
    • Massey, J.B.1
  • 23
    • 33748249320 scopus 로고    scopus 로고
    • Structures of biologically active oxysterols determine their differential effects on phospholipid membranes
    • Massey, J.B.; Pownall, H.J. Structures of biologically active oxysterols determine their differential effects on phospholipid membranes. Biochemistry 2006, 45, 10747-10758.
    • (2006) Biochemistry , vol.45 , pp. 10747-10758
    • Massey, J.B.1    Pownall, H.J.2
  • 24
    • 67349262029 scopus 로고    scopus 로고
    • Interactions of oxysterols with membranes and proteins
    • Olkkonen, V.M.; Hynynen, R. Interactions of oxysterols with membranes and proteins. Mol. Aspects Med. 2009, 30, 123-133.
    • (2009) Mol. Aspects Med. , vol.30 , pp. 123-133
    • Olkkonen, V.M.1    Hynynen, R.2
  • 25
    • 63249096864 scopus 로고    scopus 로고
    • Oxysterols and mechanisms of apoptotic signaling: Implications in the pathology of degenerative diseases
    • Lordan, S.; Mackrill, J.J.; O'Brien, N.M. Oxysterols and mechanisms of apoptotic signaling: Implications in the pathology of degenerative diseases. J. Nutr. Biochem. 2009, 20, 321-336.
    • (2009) J. Nutr. Biochem. , vol.20 , pp. 321-336
    • Lordan, S.1    Mackrill, J.J.2    O'brien, N.M.3
  • 26
    • 84866325411 scopus 로고    scopus 로고
    • Macrophage oxysterols and their binding proteins: Roles in atherosclerosis
    • Olkkonen, V.M. Macrophage oxysterols and their binding proteins: Roles in atherosclerosis. Curr. Opin. Lipidol. 2012, 23, 462-470.
    • (2012) Curr. Opin. Lipidol. , vol.23 , pp. 462-470
    • Olkkonen, V.M.1
  • 27
    • 77958057683 scopus 로고    scopus 로고
    • Macrophages, oxysterols and atherosclerosis
    • Shibata, N.; Glass, C.K. Macrophages, oxysterols and atherosclerosis. Circ. J. 2010, 74, 2045-2051.
    • (2010) Circ. J. , vol.74 , pp. 2045-2051
    • Shibata, N.1    Glass, C.K.2
  • 28
    • 52949150827 scopus 로고    scopus 로고
    • Side effects of oxysterols: Cytotoxicity, oxidation, inflammation, and phospholipidosis
    • Vejux, A.; Malvitte, L.; Lizard, G. Side effects of oxysterols: Cytotoxicity, oxidation, inflammation, and phospholipidosis. Braz J. Med. Biol. Res. 2008, 41, 545-556.
    • (2008) Braz J. Med. Biol. Res. , vol.41 , pp. 545-556
    • Vejux, A.1    Malvitte, L.2    Lizard, G.3
  • 29
    • 0034961072 scopus 로고    scopus 로고
    • Good cholesterol, bad cholesterol: Role of oxysterols in biliary tract diseases
    • Wang, D.Q.; Afdhal, N.H. Good cholesterol, bad cholesterol: Role of oxysterols in biliary tract diseases. Gastroenterology 2001, 121, 216-218.
    • (2001) Gastroenterology , vol.121 , pp. 216-218
    • Wang, D.Q.1    Afdhal, N.H.2
  • 30
    • 37649021073 scopus 로고    scopus 로고
    • Oxysterols: Novel biologic roles for the 21st century
    • Javitt, N.B. Oxysterols: Novel biologic roles for the 21st century. Steroids 2008, 73, 149-157.
    • (2008) Steroids , vol.73 , pp. 149-157
    • Javitt, N.B.1
  • 32
    • 0035108917 scopus 로고    scopus 로고
    • Overlapping functions of the yeast oxysterol-binding protein homologues
    • Beh, C.T.; Cool, L.; Phillips, J.; Rine, J. Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 2001, 157, 1117-1140.
    • (2001) Genetics , vol.157 , pp. 1117-1140
    • Beh, C.T.1    Cool, L.2    Phillips, J.3    Rine, J.4
  • 33
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Im, Y.J.; Raychaudhuri, S.; Prinz, W.A.; Hurley, J.H. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 2005, 437, 154-158.
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 34
    • 0035885867 scopus 로고    scopus 로고
    • A family of 12 human genes containing oxysterol-binding domains
    • Jaworski, C.J.; Moreira, E.; Li, A.; Lee, R.; Rodriguez, I.R. A family of 12 human genes containing oxysterol-binding domains. Genomics 2001, 78, 185-196.
    • (2001) Genomics , vol.78 , pp. 185-196
    • Jaworski, C.J.1    Moreira, E.2    Li, A.3    Lee, R.4    Rodriguez, I.R.5
  • 36
    • 84884293024 scopus 로고    scopus 로고
    • Oxysterol-binding proteins: Sterol and phosphoinositide sensors coordinating transport, signaling and metabolism
    • Olkkonen, V.M.; Li, S. Oxysterol-binding proteins: Sterol and phosphoinositide sensors coordinating transport, signaling and metabolism. Prog. Lipid Res. 2013, 52, 529-538.
    • (2013) Prog. Lipid Res. , vol.52 , pp. 529-538
    • Olkkonen, V.M.1    Li, S.2
  • 37
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    • Raychaudhuri, S.; Im, Y.J.; Hurley, J.H.; Prinz, W.A. Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides. J. Cell. Biol. 2006, 173, 107-119.
    • (2006) J. Cell. Biol. , vol.173 , pp. 107-119
    • Raychaudhuri, S.1    Im, Y.J.2    Hurley, J.H.3    Prinz, W.A.4
  • 38
  • 39
    • 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.; Sullivan, D.P.; Kersting, M.C.; Dittman, J.S.; Beh, C.T.; Menon, A.K. Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM. Traffic 2011, 12, 1341-1355.
    • (2011) Traffic , vol.12 , pp. 1341-1355
    • Georgiev, A.G.1    Sullivan, D.P.2    Kersting, M.C.3    Dittman, J.S.4    Beh, C.T.5    Menon, A.K.6
  • 40
    • 0024422669 scopus 로고
    • CDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper
    • Dawson, P.A.; Ridgway, N.D.; Slaughter, C.A.; Brown, M.S.; Goldstein, J.L. cDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper. J. Biol. Chem. 1989, 264, 16798-16803.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16798-16803
    • Dawson, P.A.1    Ridgway, N.D.2    Slaughter, C.A.3    Brown, M.S.4    Goldstein, J.L.5
  • 41
    • 0026564767 scopus 로고
    • Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding
    • Ridgway, N.D.; Dawson, P.A.; Ho, Y.K.; Brown, M.S.; Goldstein, J.L. Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding. J. Cell. Biol. 1992, 116, 307-319.
    • (1992) J. Cell. Biol. , vol.116 , pp. 307-319
    • Ridgway, N.D.1    Dawson, P.A.2    Ho, Y.K.3    Brown, M.S.4    Goldstein, J.L.5
  • 42
    • 0021747172 scopus 로고
    • Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
    • Taylor, F.R.; Saucier, S.E.; Shown, E.P.; Parish, E.J.; Kandutsch, A.A. Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase. J. Biol. Chem. 1984, 259, 12382-12387.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12382-12387
    • Taylor, F.R.1    Saucier, S.E.2    Shown, E.P.3    Parish, E.J.4    Kandutsch, A.A.5
  • 43
    • 0036472330 scopus 로고    scopus 로고
    • Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments
    • Wang, C.; JeBailey, L.; Ridgway, N.D. Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments. Biochem. J. 2002, 361, 461-472.
    • (2002) Biochem. J. , vol.361 , pp. 461-472
    • Wang, C.1    Jebailey, L.2    Ridgway, N.D.3
  • 44
    • 43149086626 scopus 로고    scopus 로고
    • N-terminus controls sterol binding while c-terminus regulates scaffolding function of OSBP
    • Wang, P.Y.; Weng, J.; Lee, S.; Anderson, R.G. N-terminus controls sterol binding while c-terminus regulates scaffolding function of OSBP. J. Biol. Chem. 2007, 283, 8034-8045.
    • (2007) J. Biol. Chem. , vol.283 , pp. 8034-8045
    • Wang, P.Y.1    Weng, J.2    Lee, S.3    Anderson, R.G.4
  • 45
    • 67650538350 scopus 로고    scopus 로고
    • OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids
    • Hynynen, R.; Suchanek, M.; Spandl, J.; Back, N.; Thiele, C.; Olkkonen, V.M. OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids. J. Lipid Res. 2009, 50, 1305-1315.
    • (2009) J. Lipid Res. , vol.50 , pp. 1305-1315
    • Hynynen, R.1    Suchanek, M.2    Spandl, J.3    Back, N.4    Thiele, C.5    Olkkonen, V.M.6
  • 47
    • 84865829993 scopus 로고    scopus 로고
    • ORP10, a cholesterol binding protein associated with microtubules, regulates apolipoprotein B-100 secretion
    • Nissilä, E.; Ohsaki, Y.; Weber-Boyvat, M.; Perttilä, J.; Ikonen, E.; Olkkonen, V.M. ORP10, a cholesterol binding protein associated with microtubules, regulates apolipoprotein B-100 secretion. Biochim. Biophys. Acta 2012, 1821, 1472-1484.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1472-1484
    • Nissilä, E.1    Ohsaki, Y.2    Weber-Boyvat, M.3    Perttilä, J.4    Ikonen, E.5    Olkkonen, V.M.6
  • 50
    • 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. 2009, 20, 1388-1399.
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 1388-1399
    • Ngo, M.1    Ridgway, N.D.2
  • 52
    • 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. 2013, 70, 3405-3421.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 3405-3421
    • Mesmin, B.1    Antonny, B.2    Drin, G.3
  • 53
    • 0029803610 scopus 로고    scopus 로고
    • Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis
    • Fang, M.; Kearns, B.G.; Gedvilaite, A.; Kagiwada, S.; Kearns, M.; Fung, M.K.; Bankaitis, V.A. Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. Embo. J. 1996, 15, 6447-6459.
    • (1996) Embo. J. , vol.15 , pp. 6447-6459
    • Fang, M.1    Kearns, B.G.2    Gedvilaite, A.3    Kagiwada, S.4    Kearns, M.5    Fung, M.K.6    Bankaitis, V.A.7
  • 54
    • 0036544518 scopus 로고    scopus 로고
    • Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex
    • Li, X.; Rivas, M.P.; Fang, M.; Marchena, J.; Mehrotra, B.; Chaudhary, A.; Feng, L.; Prestwich, G.D.; Bankaitis, V.A. Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. J. Cell. Biol. 2002, 157, 63-77.
    • (2002) J. Cell. Biol. , vol.157 , pp. 63-77
    • Li, X.1    Rivas, M.P.2    Fang, M.3    Marchena, J.4    Mehrotra, B.5    Chaudhary, A.6    Feng, L.7    Prestwich, G.D.8    Bankaitis, V.A.9
  • 56
    • 80053594641 scopus 로고    scopus 로고
    • The sterol-binding protein Kes1/Osh4p is a regulator of polarized exocytosis
    • Alfaro, G.; Johansen, J.; Dighe, S.A.; Duamel, G.; Kozminski, K.G.; Beh, C.T. The sterol-binding protein Kes1/Osh4p is a regulator of polarized exocytosis. Traffic 2011, 12, 1521-1536.
    • (2011) Traffic , vol.12 , pp. 1521-1536
    • Alfaro, G.1    Johansen, J.2    Dighe, S.A.3    Duamel, G.4    Kozminski, K.G.5    Beh, C.T.6
  • 58
    • 84879814659 scopus 로고    scopus 로고
    • Structure of osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins
    • Tong, J.; Yang, H.; Eom, S.H.; Im, Y.J. Structure of osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins. Structure 2013, 21, 1203-1213.
    • (2013) Structure , vol.21 , pp. 1203-1213
    • Tong, J.1    Yang, H.2    Eom, S.H.3    Im, Y.J.4
  • 59
    • 84884210112 scopus 로고    scopus 로고
    • Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins
    • doi:10.1038/nature12430
    • Maeda K.; Anand, K.; Chiapparino, A.; Kumar, A.; Poletto, M.; Kaksonen, M.; Gavin, A.C. Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins. Nature 2013, doi:10.1038/nature12430.
    • (2013) Nature
    • Maeda, K.1    Anand, K.2    Chiapparino, A.3    Kumar, A.4    Poletto, M.5    Kaksonen, M.6    Gavin, A.C.7
  • 60
    • 25444460845 scopus 로고    scopus 로고
    • Molecular characterization of Osh6p, an oxysterol binding protein homolog in the yeast Saccharomyces cerevisiae
    • Wang, P.; Duan, W.; Munn, A.L.; Yang, H. Molecular characterization of Osh6p, an oxysterol binding protein homolog in the yeast Saccharomyces cerevisiae. FEBS J. 2005, 272, 4703-4715.
    • (2005) FEBS J. , vol.272 , pp. 4703-4715
    • Wang, P.1    Duan, W.2    Munn, A.L.3    Yang, H.4
  • 61
    • 33947719759 scopus 로고    scopus 로고
    • Characterization of the sterol-binding domain of oxysterol-binding protein (OSBP)-related protein 4 reveals a novel role in vimentin organization
    • Wyles, J.P.; Perry, R.J.; Ridgway, N.D. Characterization of the sterol-binding domain of oxysterol-binding protein (OSBP)-related protein 4 reveals a novel role in vimentin organization. Exp. Cell. Res. 2007, 313, 1426-1437.
    • (2007) Exp. Cell. Res. , vol.313 , pp. 1426-1437
    • Wyles, J.P.1    Perry, R.J.2    Ridgway, N.D.3
  • 64
    • 8744254603 scopus 로고    scopus 로고
    • Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae
    • Kvam, E.; Goldfarb, D.S. Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae. J. Cell. Sci. 2004, 117, 4959-4968.
    • (2004) J. Cell. Sci. , vol.117 , pp. 4959-4968
    • Kvam, E.1    Goldfarb, D.S.2
  • 65
    • 0035163224 scopus 로고    scopus 로고
    • Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction
    • Levine, T.P.; Munro, S. Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol. Biol. Cell. 2001, 12, 1633-1644.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 66
    • 2342637722 scopus 로고    scopus 로고
    • Oxysterol binding proteins: In more than one place at one time? Biochem
    • Olkkonen, V.M.; Levine, T.P. Oxysterol binding proteins: in more than one place at one time? Biochem. Cell Biol. 2004, 82, 87-98.
    • (2004) Cell Biol. , vol.82 , pp. 87-98
    • Olkkonen, V.M.1    Levine, T.P.2
  • 67
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • Stefan, C.J.; Manford, A.G.; Baird, D.; Yamada-Hanff, J.; Mao, Y.; Emr, S.D. Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites. Cell 2011, 144, 389-401.
    • (2011) Cell , vol.144 , pp. 389-401
    • Stefan, C.J.1    Manford, A.G.2    Baird, D.3    Yamada-Hanff, J.4    Mao, Y.5    Emr, S.D.6
  • 68
    • 0035023874 scopus 로고    scopus 로고
    • A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids
    • Pichler, H.; Gaigg, B.; Hrastnik, C.; Achleitner, G.; Kohlwein, S.D.; Zellnig, G.; Perktold, A.; Daum, G. A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids. Eur. J. Biochem. 2001, 268, 2351-2361.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2351-2361
    • Pichler, H.1    Gaigg, B.2    Hrastnik, C.3    Achleitner, G.4    Kohlwein, S.D.5    Zellnig, G.6    Perktold, A.7    Daum, G.8
  • 70
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • Johansson, M.; Lehto, M.; Tanhuanpää, K.; Cover, T.L.; Olkkonen, V.M. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol. Biol. Cell. 2005, 16, 5480-5492.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpää, K.3    Cover, T.L.4    Olkkonen, V.M.5
  • 71
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • Rocha, N.; Kuijl, C.; van der Kant, R.; Janssen, L.; Houben, D.; Janssen, H.; Zwart, W.; Neefjes, J. Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. J. Cell. Biol. 2009, 185, 1209-1225.
    • (2009) J. Cell. Biol. , vol.185 , pp. 1209-1225
    • Rocha, N.1    Kuijl, C.2    Van Der Kant, R.3    Janssen, L.4    Houben, D.5    Janssen, H.6    Zwart, W.7    Neefjes, J.8
  • 72
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin
    • Johansson, M.; Rocha, N.; Zwart, W.; Jordens, I.; Janssen, L.; Kuijl, C.; Olkkonen, V.M.; Neefjes, J. Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin. J. Cell. Biol. 2007, 176, 459-471.
    • (2007) J. Cell. Biol. , vol.176 , pp. 459-471
    • Johansson, M.1    Rocha, N.2    Zwart, W.3    Jordens, I.4    Janssen, L.5    Kuijl, C.6    Olkkonen, V.M.7    Neefjes, J.8


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