메뉴 건너뛰기




Volumn 52, Issue 4, 2013, Pages 529-538

Oxysterol-binding proteins: Sterol and phosphoinositide sensors coordinating transport, signaling and metabolism

Author keywords

Cell signaling; Lipid metabolism; Membrane contact site; ORP; OSBP; Oxysterol

Indexed keywords

APOLIPOPROTEIN B100; CELL MEMBRANE PROTEIN; FAT DROPLET; HIGH DENSITY LIPOPROTEIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; OXYSTEROL BINDING PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PHOSPHOLIPID BINDING PROTEIN; PROTEIN ORP10; PROTEIN ORP11; PROTEIN ORP1L; PROTEIN ORP2; PROTEIN ORP3; PROTEIN ORP4; PROTEIN ORP5; PROTEIN ORP8; SPHINGOMYELIN; STEROL; UNCLASSIFIED DRUG;

EID: 84884293024     PISSN: 01637827     EISSN: 18732194     Source Type: Journal    
DOI: 10.1016/j.plipres.2013.06.004     Document Type: Review
Times cited : (135)

References (136)
  • 4
    • 84862192727 scopus 로고    scopus 로고
    • Vesicle-mediated ER export of proteins and lipids
    • A.D. Gillon, C.F. Latham, and E.A. Miller Vesicle-mediated ER export of proteins and lipids Biochim Biophys Acta 1821 2012 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
    • G. van Meer, and H. Sprong Membrane lipids and vesicular traffic Curr Opin Cell Biol 16 2004 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
    • S. Lev Non-vesicular lipid transport by lipid-transfer proteins and beyond Nat Rev Mol Cell Biol 11 2010 739 750
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 739-750
    • Lev, S.1
  • 9
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    • S. Raychaudhuri, Y.J. Im, J.H. Hurley, and W.A. Prinz Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides J Cell Biol 173 2006 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
  • 10
    • 57349090688 scopus 로고    scopus 로고
    • Nonvesicular phospholipid transfer between peroxisomes and the endoplasmic reticulum
    • S. Raychaudhuri, and W.A. Prinz Nonvesicular phospholipid transfer between peroxisomes and the endoplasmic reticulum Proc Natl Acad Sci USA 105 2008 15785 15790
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15785-15790
    • Raychaudhuri, S.1    Prinz, W.A.2
  • 11
    • 0021099854 scopus 로고
    • Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane
    • R.G. Sleight, and R.E. Pagano Rapid appearance of newly synthesized phosphatidylethanolamine at the plasma membrane J Biol Chem 258 1983 9050 9058
    • (1983) J Biol Chem , vol.258 , pp. 9050-9058
    • Sleight, R.G.1    Pagano, R.E.2
  • 12
    • 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
    • P.J. Trotter, W.I. Wu, J. Pedretti, R. Yates, and D.R. Voelker A genetic screen for aminophospholipid transport mutants identifies the phosphatidylinositol 4-kinase, STT4p, as an essential component in phosphatidylserine metabolism J Biol Chem 273 1998 13189 13196
    • (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
  • 13
    • 0026088027 scopus 로고
    • Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum
    • J.E. Vance Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum J Biol Chem 266 1991 89 97
    • (1991) J Biol Chem , vol.266 , pp. 89-97
    • Vance, J.E.1
  • 14
    • 0025917178 scopus 로고
    • Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites for synthesis to the cell surface
    • J.E. Vance, E.J. Aasman, and R. Szarka Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites for synthesis to the cell surface J Biol Chem 266 1991 8241 8247
    • (1991) J Biol Chem , vol.266 , pp. 8241-8247
    • Vance, J.E.1    Aasman, E.J.2    Szarka, R.3
  • 16
    • 33745755614 scopus 로고    scopus 로고
    • Inter-organelle membrane contact sites: Through a glass, darkly
    • T. Levine, and C. Loewen Inter-organelle membrane contact sites: through a glass, darkly Curr Opin Cell Biol 18 2006 371 378
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 371-378
    • Levine, T.1    Loewen, C.2
  • 17
    • 80755153578 scopus 로고    scopus 로고
    • Staying in touch: The molecular era of organelle contact sites
    • Y. Elbaz, and M. Schuldiner Staying in touch: the molecular era of organelle contact sites Trends Biochem Sci 36 2011 616 623
    • (2011) Trends Biochem Sci , vol.36 , pp. 616-623
    • Elbaz, Y.1    Schuldiner, M.2
  • 18
    • 84883451938 scopus 로고    scopus 로고
    • ER-PM connections: Sites of information transfer and inter-organelle communication
    • doi: pii: S0955-0674(13)00043-4. 10.1016/j.ceb.2013.02.020
    • C.J. Stefan, A.G. Manford, and S.D. Emr ER-PM connections: sites of information transfer and inter-organelle communication Curr Opin Cell Biol Mar 19 2013 doi: pii: S0955-0674(13)00043-4. 10.1016/j.ceb.2013.02.020
    • (2013) Curr Opin Cell Biol , Issue.MAR 19
    • Stefan, C.J.1    Manford, A.G.2    Emr, S.D.3
  • 19
    • 79960739849 scopus 로고    scopus 로고
    • Lipid transfer and signaling at organelle contact sites: The tip of the iceberg
    • A. Toulmay, and W.A. Prinz Lipid transfer and signaling at organelle contact sites: the tip of the iceberg Curr Opin Cell Biol 23 2011 458 463
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 458-463
    • Toulmay, A.1    Prinz, W.A.2
  • 22
    • 0035108917 scopus 로고    scopus 로고
    • Overlapping functions of the yeast oxysterol-binding protein homologues
    • C.T. Beh, L. Cool, J. Phillips, and J. Rine Overlapping functions of the yeast oxysterol-binding protein homologues Genetics 157 2001 1117 1140
    • (2001) Genetics , vol.157 , pp. 1117-1140
    • Beh, C.T.1    Cool, L.2    Phillips, J.3    Rine, J.4
  • 23
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Y.J. Im, S. Raychaudhuri, W.A. Prinz, and J.H. Hurley Structural mechanism for sterol sensing and transport by OSBP-related proteins Nature 437 2005 154 158
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 24
    • 0035885867 scopus 로고    scopus 로고
    • A family of 12 human genes containing oxysterol-binding domains
    • C.J. Jaworski, E. Moreira, A. Li, R. Lee, and I.R. Rodriguez A family of 12 human genes containing oxysterol-binding domains Genomics 78 2001 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
  • 27
    • 0024422669 scopus 로고
    • CDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper
    • P.A. Dawson, N.D. Ridgway, C.A. Slaughter, M.S. Brown, and J.L. Goldstein cDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper J Biol Chem 264 1989 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
  • 28
    • 0026564767 scopus 로고
    • Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding
    • N.D. Ridgway, P.A. Dawson, Y.K. Ho, M.S. Brown, and J.L. Goldstein Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding J Cell Biol 116 1992 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
  • 29
    • 0036472330 scopus 로고    scopus 로고
    • Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments
    • C. Wang, L. JeBailey, and N.D. Ridgway Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments Biochem J 361 2002 461 472
    • (2002) Biochem J , vol.361 , pp. 461-472
    • Wang, C.1    Jebailey, L.2    Ridgway, N.D.3
  • 30
    • 43149086626 scopus 로고    scopus 로고
    • N-terminus controls sterol binding while c-terminus regulates scaffolding function of OSBP
    • P.Y. Wang, J. Weng, S. Lee, and R.G. Anderson N-terminus controls sterol binding while c-terminus regulates scaffolding function of OSBP J Biol Chem 283 2007 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
  • 31
    • 67650538350 scopus 로고    scopus 로고
    • OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids
    • R. Hynynen, M. Suchanek, J. Spandl, N. Back, C. Thiele, and V.M. Olkkonen OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids J Lipid Res 50 2009 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
  • 32
    • 34547439826 scopus 로고    scopus 로고
    • The mammalian OSBP-related proteins (ORP) bind 25-hydroxycholesterol in an evolutionarily conserved pocket
    • M. Suchanek, R. Hynynen, G. Wohlfahrt, M. Lehto, M. Johansson, and H. Saarinen The mammalian OSBP-related proteins (ORP) bind 25-hydroxycholesterol in an evolutionarily conserved pocket Biochem J 405 3 2007 473 480
    • (2007) Biochem J , vol.405 , Issue.3 , pp. 473-480
    • Suchanek, M.1    Hynynen, R.2    Wohlfahrt, G.3    Lehto, M.4    Johansson, M.5    Saarinen, H.6
  • 33
    • 84865829993 scopus 로고    scopus 로고
    • ORP10, a cholesterol binding protein associated with microtubules, regulates apolipoprotein B-100 secretion
    • E. Nissilä, Y. Ohsaki, M. Weber-Boyvat, J. Perttilä, E. Ikonen, and V.M. Olkkonen ORP10, a cholesterol binding protein associated with microtubules, regulates apolipoprotein B-100 secretion Biochim Biophys Acta 1821 12 2012 1472 1484
    • (2012) Biochim Biophys Acta , vol.1821 , Issue.12 , pp. 1472-1484
    • Nissilä, E.1    Ohsaki, Y.2    Weber-Boyvat, M.3    Perttilä, J.4    Ikonen, E.5    Olkkonen, V.M.6
  • 35
    • 14644391519 scopus 로고    scopus 로고
    • OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation
    • P.Y. Wang, J. Weng, and R.G. Anderson OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation Science 307 2005 1472 1476
    • (2005) Science , vol.307 , pp. 1472-1476
    • Wang, P.Y.1    Weng, J.2    Anderson, R.G.3
  • 36
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • C.J. Loewen, A. Roy, and T.P. Levine A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP Embo J 22 2003 2025 2035
    • (2003) Embo J , vol.22 , pp. 2025-2035
    • Loewen, C.J.1    Roy, A.2    Levine, T.P.3
  • 37
    • 78651328466 scopus 로고    scopus 로고
    • A role for oxysterol-binding protein-related protein 5 in endosomal cholesterol trafficking
    • X. Du, J. Kumar, C. Ferguson, T.A. Schulz, Y.S. Ong, and W. Hong A role for oxysterol-binding protein-related protein 5 in endosomal cholesterol trafficking J Cell Biol 192 2011 121 135
    • (2011) J Cell Biol , vol.192 , pp. 121-135
    • Du, X.1    Kumar, J.2    Ferguson, C.3    Schulz, T.A.4    Ong, Y.S.5    Hong, W.6
  • 38
    • 38049136886 scopus 로고    scopus 로고
    • OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and cholesterol efflux from macrophages
    • D. Yan, M.I. Mäyränpää, J. Wong, J. Perttilä, M. Lehto, and M. Jauhiainen OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and cholesterol efflux from macrophages J Biol Chem 283 2008 332 340
    • (2008) J Biol Chem , vol.283 , pp. 332-340
    • Yan, D.1    Mäyränpää, M.I.2    Wong, J.3    Perttilä, J.4    Lehto, M.5    Jauhiainen, M.6
  • 39
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes
    • T.P. Levine, and S. Munro The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes Curr Biol 8 1998 729 739
    • (1998) Curr Biol , vol.8 , pp. 729-739
    • Levine, T.P.1    Munro, S.2
  • 40
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • M. Johansson, M. Lehto, K. Tanhuanpää, T.L. Cover, and V.M. Olkkonen The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments Mol Biol Cell 16 2005 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
  • 41
    • 26844518949 scopus 로고    scopus 로고
    • Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants
    • M. Lehto, R. Hynynen, K. Karjalainen, E. Kuismanen, K. Hyvärinen, and V.M. Olkkonen Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants Exp Cell Res 310 2005 445 462
    • (2005) Exp Cell Res , vol.310 , pp. 445-462
    • Lehto, M.1    Hynynen, R.2    Karjalainen, K.3    Kuismanen, E.4    Hyvärinen, K.5    Olkkonen, V.M.6
  • 42
    • 65249161758 scopus 로고    scopus 로고
    • Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function
    • M. Ngo, and N.D. Ridgway Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function Mol Biol Cell 20 2009 1388 1399
    • (2009) Mol Biol Cell , vol.20 , pp. 1388-1399
    • Ngo, M.1    Ridgway, N.D.2
  • 43
    • 18844430347 scopus 로고    scopus 로고
    • Identification and assessment of the role of a nominal phospholipid binding region of ORP1S (oxysterol-binding-protein-related protein 1 short) in the regulation of vesicular transport
    • G.D. Fairn, and C.R. McMaster Identification and assessment of the role of a nominal phospholipid binding region of ORP1S (oxysterol-binding-protein- related protein 1 short) in the regulation of vesicular transport Biochem J 387 2005 889 896
    • (2005) Biochem J , vol.387 , pp. 889-896
    • Fairn, G.D.1    McMaster, C.R.2
  • 44
    • 23944475081 scopus 로고    scopus 로고
    • Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis
    • R. Hynynen, S. Laitinen, R. Käkelä, K. Tanhuanpää, S. Lusa, and C. Ehnholm Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis Biochem J 390 2005 273 283
    • (2005) Biochem J , vol.390 , pp. 273-283
    • Hynynen, R.1    Laitinen, S.2    Käkelä, R.3    Tanhuanpää, K.4    Lusa, S.5    Ehnholm, C.6
  • 45
    • 74049122402 scopus 로고    scopus 로고
    • Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues
    • T.A. Schulz, M.G. Choi, S. Raychaudhuri, J.A. Mears, R. Ghirlando, and J.E. Hinshaw Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues J Cell Biol 187 2009 889 903
    • (2009) J Cell Biol , vol.187 , pp. 889-903
    • Schulz, T.A.1    Choi, M.G.2    Raychaudhuri, S.3    Mears, J.A.4    Ghirlando, R.5    Hinshaw, J.E.6
  • 46
    • 80053594641 scopus 로고    scopus 로고
    • The sterol-binding protein Kes1/Osh4p is a regulator of polarized exocytosis
    • G. Alfaro, J. Johansen, S.A. Dighe, G. Duamel, K.G. Kozminski, and C.T. Beh The sterol-binding protein Kes1/Osh4p is a regulator of polarized exocytosis Traffic 12 2011 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
  • 47
    • 80052630805 scopus 로고    scopus 로고
    • Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM
    • A.G. Georgiev, D.P. Sullivan, M.C. Kersting, J.S. Dittman, C.T. Beh, and A.K. Menon Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM Traffic 12 2011 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
  • 48
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46 50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 49
    • 8744254603 scopus 로고    scopus 로고
    • Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae
    • E. Kvam, and D.S. Goldfarb Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae J Cell Sci 117 2004 4959 4968
    • (2004) J Cell Sci , vol.117 , pp. 4959-4968
    • Kvam, E.1    Goldfarb, D.S.2
  • 50
    • 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
    • T.P. Levine, and S. Munro Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction Mol Biol Cell 12 2001 1633 1644
    • (2001) Mol Biol Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 51
    • 2342637722 scopus 로고    scopus 로고
    • Oxysterol binding proteins: In more than one place at one time?
    • V.M. Olkkonen, and T.P. Levine Oxysterol binding proteins: in more than one place at one time? Biochem Cell Biol 82 2004 87 98
    • (2004) Biochem Cell Biol , vol.82 , pp. 87-98
    • Olkkonen, V.M.1    Levine, T.P.2
  • 52
    • 78651076417 scopus 로고    scopus 로고
    • Role of ORPs in sterol transport from plasma membrane to ER and lipid droplets in mammalian cells
    • M. Jansen, Y. Ohsaki, L. Rita Rega, R. Bittman, V.M. Olkkonen, and E. Ikonen Role of ORPs in sterol transport from plasma membrane to ER and lipid droplets in mammalian cells Traffic 12 2011 218 231
    • (2011) Traffic , vol.12 , pp. 218-231
    • Jansen, M.1    Ohsaki, Y.2    Rita Rega, L.3    Bittman, R.4    Olkkonen, V.M.5    Ikonen, E.6
  • 53
    • 84874105781 scopus 로고    scopus 로고
    • Modification of the lipidome in RAW264.7 macrophage subjected to stable silencing of oxysterol-binding proteins
    • T. Vihervaara, R. Käkelä, G. Liebisch, K. Tarasov, G. Schmitz, and V.M. Olkkonen Modification of the lipidome in RAW264.7 macrophage subjected to stable silencing of oxysterol-binding proteins Biochimie 95 2012 538 547
    • (2012) Biochimie , vol.95 , pp. 538-547
    • Vihervaara, T.1    Käkelä, R.2    Liebisch, G.3    Tarasov, K.4    Schmitz, G.5    Olkkonen, V.M.6
  • 54
    • 0032895139 scopus 로고    scopus 로고
    • Chinese hamster ovary cells overexpressing the oxysterol binding protein (OSBP) display enhanced synthesis of sphingomyelin in response to 25-hydroxycholesterol
    • T.A. Lagace, D.M. Byers, H.W. Cook, and N.D. Ridgway Chinese hamster ovary cells overexpressing the oxysterol binding protein (OSBP) display enhanced synthesis of sphingomyelin in response to 25-hydroxycholesterol J Lipid Res 40 1999 109 116
    • (1999) J Lipid Res , vol.40 , pp. 109-116
    • Lagace, T.A.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 55
    • 33744728346 scopus 로고    scopus 로고
    • Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein
    • R.J. Perry, and N.D. Ridgway Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein Mol Biol Cell 17 2006 2604 2616
    • (2006) Mol Biol Cell , vol.17 , pp. 2604-2616
    • Perry, R.J.1    Ridgway, N.D.2
  • 56
    • 0021747172 scopus 로고
    • Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
    • F.R. Taylor, S.E. Saucier, E.P. Shown, E.J. Parish, and A.A. Kandutsch Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase J Biol Chem 259 1984 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
  • 58
    • 0032553324 scopus 로고    scopus 로고
    • Differential effects of sphingomyelin hydrolysis and cholesterol transport on oxysterol-binding protein phosphorylation and Golgi localization
    • N.D. Ridgway, T.A. Lagace, H.W. Cook, and D.M. Byers Differential effects of sphingomyelin hydrolysis and cholesterol transport on oxysterol-binding protein phosphorylation and Golgi localization J Biol Chem 273 1998 31621 31628
    • (1998) J Biol Chem , vol.273 , pp. 31621-31628
    • Ridgway, N.D.1    Lagace, T.A.2    Cook, H.W.3    Byers, D.M.4
  • 59
    • 0032533161 scopus 로고    scopus 로고
    • Cholesterol regulates oxysterol binding protein (OSBP) phosphorylation and Golgi localization in Chinese hamster ovary cells: Correlation with stimulation of sphingomyelin synthesis by 25-hydroxycholesterol
    • M.K. Storey, D.M. Byers, H.W. Cook, and N.D. Ridgway Cholesterol regulates oxysterol binding protein (OSBP) phosphorylation and Golgi localization in Chinese hamster ovary cells: correlation with stimulation of sphingomyelin synthesis by 25-hydroxycholesterol Biochem J 336 1998 247 256
    • (1998) Biochem J , vol.336 , pp. 247-256
    • Storey, M.K.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 60
    • 23844453427 scopus 로고    scopus 로고
    • Inhibition of cholesterol biosynthesis by 25-hydroxycholesterol is independent of OSBP
    • T. Nishimura, T. Inoue, N. Shibata, A. Sekine, W. Takabe, and N. Noguchi Inhibition of cholesterol biosynthesis by 25-hydroxycholesterol is independent of OSBP Genes Cells 10 2005 793 801
    • (2005) Genes Cells , vol.10 , pp. 793-801
    • Nishimura, T.1    Inoue, T.2    Shibata, N.3    Sekine, A.4    Takabe, W.5    Noguchi, N.6
  • 61
    • 14744294236 scopus 로고    scopus 로고
    • Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function
    • V. Litvak, N. Dahan, S. Ramachandran, H. Sabanay, and S. Lev Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function Nat Cell Biol 7 2005 225 234
    • (2005) Nat Cell Biol , vol.7 , pp. 225-234
    • Litvak, V.1    Dahan, N.2    Ramachandran, S.3    Sabanay, H.4    Lev, S.5
  • 62
    • 55549111249 scopus 로고    scopus 로고
    • Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport
    • D. Peretti, N. Dahan, E. Shimoni, K. Hirschberg, and S. Lev Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport Mol Biol Cell 19 2008 3871 3884
    • (2008) Mol Biol Cell , vol.19 , pp. 3871-3884
    • Peretti, D.1    Dahan, N.2    Shimoni, E.3    Hirschberg, K.4    Lev, S.5
  • 63
    • 77954204064 scopus 로고    scopus 로고
    • Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation
    • S. Nhek, M. Ngo, X. Yang, M.M. Ng, S.J. Field, and J.M. Asara Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation Mol Biol Cell 21 2010 2327 2337
    • (2010) Mol Biol Cell , vol.21 , pp. 2327-2337
    • Nhek, S.1    Ngo, M.2    Yang, X.3    Ng, M.M.4    Field, S.J.5    Asara, J.M.6
  • 64
    • 34347379940 scopus 로고    scopus 로고
    • Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
    • T. Fugmann, A. Hausser, P. Schoffler, S. Schmid, K. Pfizenmaier, and M.A. Olayioye Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein J Cell Biol 178 2007 15 22
    • (2007) J Cell Biol , vol.178 , pp. 15-22
    • Fugmann, T.1    Hausser, A.2    Schoffler, P.3    Schmid, S.4    Pfizenmaier, K.5    Olayioye, M.A.6
  • 65
    • 42949170513 scopus 로고    scopus 로고
    • Oxysterol-binding protein-1 (OSBP1) modulates processing and trafficking of the amyloid precursor protein
    • C.V. Zerbinatti, J.M. Cordy, C.D. Chen, M. Guillily, S. Suon, and W.J. Ray Oxysterol-binding protein-1 (OSBP1) modulates processing and trafficking of the amyloid precursor protein Mol Neurodegener 3 2008 5
    • (2008) Mol Neurodegener , vol.3 , pp. 5
    • Zerbinatti, C.V.1    Cordy, J.M.2    Chen, C.D.3    Guillily, M.4    Suon, S.5    Ray, W.J.6
  • 66
    • 78149258099 scopus 로고    scopus 로고
    • OSBP- and FAN-mediated sterol requirement for spermatogenesis in Drosophila
    • Z. Ma, Z. Liu, and X. Huang OSBP- and FAN-mediated sterol requirement for spermatogenesis in Drosophila Development 137 2010 3775 3784
    • (2010) Development , vol.137 , pp. 3775-3784
    • Ma, Z.1    Liu, Z.2    Huang, X.3
  • 67
    • 84859601572 scopus 로고    scopus 로고
    • Membrane phospholipid asymmetry counters the adverse effects of sterol overloading in the Golgi membrane of Drosophila
    • Z. Ma, Z. Liu, and X. Huang Membrane phospholipid asymmetry counters the adverse effects of sterol overloading in the Golgi membrane of Drosophila Genetics 190 2012 1299 1308
    • (2012) Genetics , vol.190 , pp. 1299-1308
    • Ma, Z.1    Liu, Z.2    Huang, X.3
  • 68
    • 69549113556 scopus 로고    scopus 로고
    • Role of oxysterol binding protein in hepatitis C virus infection
    • Y. Amako, A. Sarkeshik, H. Hotta, J. Yates 3rd, and A. Siddiqui Role of oxysterol binding protein in hepatitis C virus infection J Virol 83 2009 9237 9246
    • (2009) J Virol , vol.83 , pp. 9237-9246
    • Amako, Y.1    Sarkeshik, A.2    Hotta, H.3    Yates III, J.4    Siddiqui, A.5
  • 69
    • 79953215325 scopus 로고    scopus 로고
    • Protein kinase D negatively regulates hepatitis C virus secretion through phosphorylation of oxysterol-binding protein and ceramide transfer protein
    • Y. Amako, G.H. Syed, and A. Siddiqui Protein kinase D negatively regulates hepatitis C virus secretion through phosphorylation of oxysterol-binding protein and ceramide transfer protein J Biol Chem 286 2011 11265 11274
    • (2011) J Biol Chem , vol.286 , pp. 11265-11274
    • Amako, Y.1    Syed, G.H.2    Siddiqui, A.3
  • 70
    • 84868138257 scopus 로고    scopus 로고
    • Phosphoinositides in the hepatitis C virus life cycle
    • B. Bishe, G. Syed, and A. Siddiqui Phosphoinositides in the hepatitis C virus life cycle Viruses 4 2012 2340 2358
    • (2012) Viruses , vol.4 , pp. 2340-2358
    • Bishe, B.1    Syed, G.2    Siddiqui, A.3
  • 71
    • 84875776334 scopus 로고    scopus 로고
    • Oxysterol-binding protein family i is the target of minor enviroxime-like compounds
    • M. Arita, H. Kojima, T. Nagano, T. Okabe, T. Wakita, and H. Shimizu Oxysterol-binding protein family I is the target of minor enviroxime-like compounds J Virol 87 2013 4252 4260
    • (2013) J Virol , vol.87 , pp. 4252-4260
    • Arita, M.1    Kojima, H.2    Nagano, T.3    Okabe, T.4    Wakita, T.5    Shimizu, H.6
  • 72
    • 84876349734 scopus 로고    scopus 로고
    • The Antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry
    • S. Amini-Bavil-Olyaee, Y.J. Choi, J.H. Lee, M. Shi, I.C. Huang, and M. Farzan The Antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry Cell Host Microbe 13 2013 452 464
    • (2013) Cell Host Microbe , vol.13 , pp. 452-464
    • Amini-Bavil-Olyaee, S.1    Choi, Y.J.2    Lee, J.H.3    Shi, M.4    Huang, I.C.5    Farzan, M.6
  • 73
    • 84855984714 scopus 로고    scopus 로고
    • Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus
    • S.D. Auweter, H.B. Yu, E.T. Arena, J.A. Guttman, and B.B. Finlay Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus Microbes Infect 14 2012 148 154
    • (2012) Microbes Infect , vol.14 , pp. 148-154
    • Auweter, S.D.1    Yu, H.B.2    Arena, E.T.3    Guttman, J.A.4    Finlay, B.B.5
  • 74
    • 0032554080 scopus 로고    scopus 로고
    • A Drosophila homologue of oxysterol binding protein (OSBP)-implications for the role of OSBP
    • L. Alphey, J. Jimenez, and D. Glover A Drosophila homologue of oxysterol binding protein (OSBP)-implications for the role of OSBP Biochim Biophys Acta 1395 1998 159 164
    • (1998) Biochim Biophys Acta , vol.1395 , pp. 159-164
    • Alphey, L.1    Jimenez, J.2    Glover, D.3
  • 75
    • 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
    • M. Fang, B.G. Kearns, A. Gedvilaite, S. Kagiwada, M. Kearns, and M.K. Fung Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis Embo J 15 1996 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
  • 76
    • 0034885330 scopus 로고    scopus 로고
    • BIP, a BRAM-interacting protein involved in TGF-beta signalling, regulates body length in Caenorhabditis elegans
    • K. Sugawara, K. Morita, N. Ueno, and H. Shibuya BIP, a BRAM-interacting protein involved in TGF-beta signalling, regulates body length in Caenorhabditis elegans Genes Cells 6 2001 599 606
    • (2001) Genes Cells , vol.6 , pp. 599-606
    • Sugawara, K.1    Morita, K.2    Ueno, N.3    Shibuya, H.4
  • 78
    • 30844437681 scopus 로고    scopus 로고
    • Docosahexaneoic acid (22:6, n-3) regulates rat hepatocyte SREBP-1 nuclear abundance by Erk- and 26S proteasome-dependent pathways
    • D. Botolin, Y. Wang, B. Christian, and D.B. Jump Docosahexaneoic acid (22:6, n-3) regulates rat hepatocyte SREBP-1 nuclear abundance by Erk- and 26S proteasome-dependent pathways J Lipid Res 47 2006 181 192
    • (2006) J Lipid Res , vol.47 , pp. 181-192
    • Botolin, D.1    Wang, Y.2    Christian, B.3    Jump, D.B.4
  • 79
    • 44349141839 scopus 로고    scopus 로고
    • Oxysterol and diabetes activate STAT3, and control endothelial expression of profilin-1 via OSBP1
    • G.R. Romeo, and A. Kazlauskas Oxysterol and diabetes activate STAT3, and control endothelial expression of profilin-1 via OSBP1 J Biol Chem 283 2008 9595 9605
    • (2008) J Biol Chem , vol.283 , pp. 9595-9605
    • Romeo, G.R.1    Kazlauskas, A.2
  • 80
    • 77954469729 scopus 로고    scopus 로고
    • Functional implications of sterol transport by the oxysterol-binding protein gene family
    • M.H. Ngo, T.R. Colbourne, and N.D. Ridgway Functional implications of sterol transport by the oxysterol-binding protein gene family Biochem J 429 2010 13 24
    • (2010) Biochem J , vol.429 , pp. 13-24
    • Ngo, M.H.1    Colbourne, T.R.2    Ridgway, N.D.3
  • 81
    • 2942703761 scopus 로고    scopus 로고
    • VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus
    • J.P. Wyles, and N.D. Ridgway VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus Exp Cell Res 297 2004 533 547
    • (2004) Exp Cell Res , vol.297 , pp. 533-547
    • Wyles, J.P.1    Ridgway, N.D.2
  • 82
    • 33845698910 scopus 로고    scopus 로고
    • Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation
    • E. Lessmann, M. Ngo, M. Leitges, S. Minguet, N.D. Ridgway, and M. Huber Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation Cell Signal 19 2007 384 392
    • (2007) Cell Signal , vol.19 , pp. 384-392
    • Lessmann, E.1    Ngo, M.2    Leitges, M.3    Minguet, S.4    Ridgway, N.D.5    Huber, M.6
  • 84
    • 84873282810 scopus 로고    scopus 로고
    • Effective killing of leukemia cells by the natural product OSW-1 through disruption of cellular calcium homeostasis
    • C. Garcia-Prieto, K.B. Riaz Ahmed, Z. Chen, Y. Zhou, N. Hammoudi, and Y. Kang Effective killing of leukemia cells by the natural product OSW-1 through disruption of cellular calcium homeostasis J Biol Chem 288 2013 3240 3250
    • (2013) J Biol Chem , vol.288 , pp. 3240-3250
    • Garcia-Prieto, C.1    Riaz Ahmed, K.B.2    Chen, Z.3    Zhou, Y.4    Hammoudi, N.5    Kang, Y.6
  • 85
    • 77952151244 scopus 로고    scopus 로고
    • Schweinfurthin A selectively inhibits proliferation and Rho signaling in glioma and neurofibromatosis type 1 tumor cells in a NF1-GRD-dependent manner
    • T.J. Turbyville, D.B. Gursel, R.G. Tuskan, J.C. Walrath, C.A. Lipschultz, and S.J. Lockett Schweinfurthin A selectively inhibits proliferation and Rho signaling in glioma and neurofibromatosis type 1 tumor cells in a NF1-GRD-dependent manner Mol Cancer Ther 9 2010 1234 1243
    • (2010) Mol Cancer Ther , vol.9 , pp. 1234-1243
    • Turbyville, T.J.1    Gursel, D.B.2    Tuskan, R.G.3    Walrath, J.C.4    Lipschultz, C.A.5    Lockett, S.J.6
  • 86
    • 0037342401 scopus 로고    scopus 로고
    • The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct
    • M. Johansson, V. Bocher, M. Lehto, G. Chinetti, E. Kuismanen, and C. Ehnholm The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct Mol Biol Cell 14 2003 903 915
    • (2003) Mol Biol Cell , vol.14 , pp. 903-915
    • Johansson, M.1    Bocher, V.2    Lehto, M.3    Chinetti, G.4    Kuismanen, E.5    Ehnholm, C.6
  • 87
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin
    • M. Johansson, N. Rocha, W. Zwart, I. Jordens, L. Janssen, and C. Kuijl Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin J Cell Biol 176 2007 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
  • 88
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • N. Rocha, C. Kuijl, R. van der Kant, L. Janssen, D. Houben, and H. Janssen Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning J Cell Biol 185 2009 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
  • 89
    • 84883382591 scopus 로고    scopus 로고
    • Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L
    • [Epub ahead of print] PMID: 23729732
    • R. van der Kant, A. Fish, L. Janssen, H. Janssen, S. Krom, and N. Ho Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L J Cell Sci May 31 2013 [Epub ahead of print] PMID: 23729732
    • (2013) J Cell Sci , Issue.MAY 31
    • Van Der Kant, R.1    Fish, A.2    Janssen, L.3    Janssen, H.4    Krom, S.5    Ho, N.6
  • 90
    • 34250873397 scopus 로고    scopus 로고
    • Expression of human OSBP-related protein 1L in macrophages enhances atherosclerotic lesion development in LDL receptor-deficient mice
    • D. Yan, M. Jauhiainen, R.B. Hildebrand, K.W. van Dijk, T.J.C. Van Berkel, and C. Ehnholm Expression of human OSBP-related protein 1L in macrophages enhances atherosclerotic lesion development in LDL receptor-deficient mice Arterioscler Thromb Vasc Biol 27 2007 1618 1624
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 1618-1624
    • Yan, D.1    Jauhiainen, M.2    Hildebrand, R.B.3    Van Dijk, K.W.4    Van Berkel, T.J.C.5    Ehnholm, C.6
  • 91
  • 92
    • 84864390310 scopus 로고    scopus 로고
    • Identification of novel host cell binding partners of Oas1b, the protein conferring resistance to flavivirus-induced disease in mice
    • S.C. Courtney, H. Di, B.M. Stockman, H. Liu, S.V. Scherbik, and M.A. Brinton Identification of novel host cell binding partners of Oas1b, the protein conferring resistance to flavivirus-induced disease in mice J Virol 86 2012 7953 7963
    • (2012) J Virol , vol.86 , pp. 7953-7963
    • Courtney, S.C.1    Di, H.2    Stockman, B.M.3    Liu, H.4    Scherbik, S.V.5    Brinton, M.A.6
  • 93
    • 77957325731 scopus 로고    scopus 로고
    • Multivesicular body formation requires OSBP-related proteins and cholesterol
    • pii: e1001055. doi: 10.1371/journal.pgen.1001055
    • H. Kobuna, T. Inoue, M. Shibata, K. Gengyo-Ando, A. Yamamoto, and S. Mitani Multivesicular body formation requires OSBP-related proteins and cholesterol PLoS Genet 6 8 2010 pii: e1001055. doi: 10.1371/journal.pgen.1001055
    • (2010) PLoS Genet , vol.6 , Issue.8
    • Kobuna, H.1    Inoue, T.2    Shibata, M.3    Gengyo-Ando, K.4    Yamamoto, A.5    Mitani, S.6
  • 94
    • 77957352699 scopus 로고    scopus 로고
    • The diverse functions of oxysterol-binding proteins
    • S. Raychaudhuri, and W.A. Prinz The diverse functions of oxysterol-binding proteins Annu Rev Cell Dev Biol 26 2010 157 177
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 157-177
    • Raychaudhuri, S.1    Prinz, W.A.2
  • 95
    • 77952314344 scopus 로고    scopus 로고
    • Oxysterol-binding proteins
    • N.D. Ridgway Oxysterol-binding proteins Subcell Biochem 51 2010 159 182
    • (2010) Subcell Biochem , vol.51 , pp. 159-182
    • Ridgway, N.D.1
  • 96
    • 84884307308 scopus 로고    scopus 로고
    • Oxysterol-binding proteins: Functions in cell regulation beyond lipid metabolism
    • doi:pii: S0006-2952(13)00120-2. 10.1016/ j.bcp.2013.02.016
    • M. Weber-Boyvat, W. Zhong, D. Yan, and V.M. Olkkonen Oxysterol-binding proteins: functions in cell regulation beyond lipid metabolism Biochem Pharmacol Feb 18 2013 doi:pii: S0006-2952(13)00120-2. 10.1016/ j.bcp.2013.02.016
    • (2013) Biochem Pharmacol , Issue.FEB 18
    • Weber-Boyvat, M.1    Zhong, W.2    Yan, D.3    Olkkonen, V.M.4
  • 97
    • 0036188574 scopus 로고    scopus 로고
    • ORP2, a homolog of oxysterol binding protein, regulates cellular cholesterol metabolism
    • S. Laitinen, M. Lehto, S. Lehtonen, K. Hyvärinen, S. Heino, and E. Lehtonen ORP2, a homolog of oxysterol binding protein, regulates cellular cholesterol metabolism J Lipid Res 43 2002 245 255
    • (2002) J Lipid Res , vol.43 , pp. 245-255
    • Laitinen, S.1    Lehto, M.2    Lehtonen, S.3    Hyvärinen, K.4    Heino, S.5    Lehtonen, E.6
  • 98
    • 84864301367 scopus 로고    scopus 로고
    • Sterol-dependent nuclear import of ORP1S promotes LXR regulated trans-activation of apoE
    • S. Lee, P.Y. Wang, Y. Jeong, D.J. Mangelsdorf, R.G. Anderson, and P. Michaely Sterol-dependent nuclear import of ORP1S promotes LXR regulated trans-activation of apoE Exp Cell Res 318 2012 2128 2142
    • (2012) Exp Cell Res , vol.318 , pp. 2128-2142
    • Lee, S.1    Wang, P.Y.2    Jeong, Y.3    Mangelsdorf, D.J.4    Anderson, R.G.5    Michaely, P.6
  • 99
    • 67349280293 scopus 로고    scopus 로고
    • Lipid droplet-organelle interactions; Sharing the fats
    • S. Murphy, S. Martin, and R.G. Parton Lipid droplet-organelle interactions; sharing the fats Biochim Biophys Acta 1791 2009 441 447
    • (2009) Biochim Biophys Acta , vol.1791 , pp. 441-447
    • Murphy, S.1    Martin, S.2    Parton, R.G.3
  • 100
    • 84866698576 scopus 로고    scopus 로고
    • OSBP-related proteins (ORPs) in human adipose depots and cultured adipocytes: Evidence for impacts on the adipocyte phenotype
    • doi: 10.1371/journal.pone.0045352
    • Y. Zhou, M. Robciuc, M. Wabitsch, A. Juuti, M. Leivonen, and C. Ehnholm OSBP-related proteins (ORPs) in human adipose depots and cultured adipocytes: evidence for impacts on the adipocyte phenotype PLoS One 7 9 2012 e45352 doi: 10.1371/journal.pone.0045352
    • (2012) PLoS One , vol.7 , Issue.9 , pp. 45352
    • Zhou, Y.1    Robciuc, M.2    Wabitsch, M.3    Juuti, A.4    Leivonen, M.5    Ehnholm, C.6
  • 101
    • 2342447668 scopus 로고    scopus 로고
    • Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: The expression and intracellular localization of ORP3, ORP6, and ORP7
    • M. Lehto, J. Tienari, S. Lehtonen, E. Lehtonen, and V.M. Olkkonen Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7 Cell Tissue Res 315 2004 39 57
    • (2004) Cell Tissue Res , vol.315 , pp. 39-57
    • Lehto, M.1    Tienari, J.2    Lehtonen, S.3    Lehtonen, E.4    Olkkonen, V.M.5
  • 106
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • C.J. Stefan, A.G. Manford, D. Baird, J. Yamada-Hanff, Y. Mao, and S.D. Emr Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites Cell 144 2011 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
  • 107
    • 80051788343 scopus 로고    scopus 로고
    • OSBP-related protein 7 interacts with GATE-16 and negatively regulates GS28 protein stability
    • W. Zhong, Y. Zhou, S. Li, T. Zhou, H. Ma, and K. Wei OSBP-related protein 7 interacts with GATE-16 and negatively regulates GS28 protein stability Exp Cell Res 317 2011 2353 2363
    • (2011) Exp Cell Res , vol.317 , pp. 2353-2363
    • Zhong, W.1    Zhou, Y.2    Li, S.3    Zhou, T.4    Ma, H.5    Wei, K.6
  • 109
    • 79958859962 scopus 로고    scopus 로고
    • OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid levels and interacts with the nucleoporin Nup62
    • 10.1371/journal.pone.0021078
    • T. Zhou, S. Li, W. Zhong, T. Vihervaara, O. Beaslas, and J. Perttila OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid levels and interacts with the nucleoporin Nup62 PLoS One 6 6 2011 e21078 10.1371/journal.pone.0021078
    • (2011) PLoS One , vol.6 , Issue.6 , pp. 21078
    • Zhou, T.1    Li, S.2    Zhong, W.3    Vihervaara, T.4    Beaslas, O.5    Perttila, J.6
  • 111
    • 84863785165 scopus 로고    scopus 로고
    • Silencing of OSBP-related protein 8 (ORP8) modifies the macrophage transcriptome, nucleoporin p62 distribution, and migration capacity
    • O. Beaslas, T. Vihervaara, J. Li, P.P. Laurila, D. Yan, and V.M. Olkkonen Silencing of OSBP-related protein 8 (ORP8) modifies the macrophage transcriptome, nucleoporin p62 distribution, and migration capacity Exp Cell Res 318 2012 1933 1945
    • (2012) Exp Cell Res , vol.318 , pp. 1933-1945
    • Beaslas, O.1    Vihervaara, T.2    Li, J.3    Laurila, P.P.4    Yan, D.5    Olkkonen, V.M.6
  • 112
    • 68549087231 scopus 로고    scopus 로고
    • Exo70-mediated recruitment of nucleoporin Nup62 at the leading edge of migrating cells is required for cell migration
    • T. Hubert, J. Vandekerckhove, and J. Gettemans Exo70-mediated recruitment of nucleoporin Nup62 at the leading edge of migrating cells is required for cell migration Traffic 10 2009 1257 1271
    • (2009) Traffic , vol.10 , pp. 1257-1271
    • Hubert, T.1    Vandekerckhove, J.2    Gettemans, J.3
  • 113
    • 79953317808 scopus 로고    scopus 로고
    • Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism
    • S.D. Jordan, M. Kruger, D.M. Willmes, N. Redemann, F.T. Wunderlich, and H.S. Bronneke Obesity-induced overexpression of miRNA-143 inhibits insulin-stimulated AKT activation and impairs glucose metabolism Nat Cell Biol 13 2011 434 446
    • (2011) Nat Cell Biol , vol.13 , pp. 434-446
    • Jordan, S.D.1    Kruger, M.2    Willmes, D.M.3    Redemann, N.4    Wunderlich, F.T.5    Bronneke, H.S.6
  • 114
    • 84875041487 scopus 로고    scopus 로고
    • Osbpl8 deficiency in mouse causes an elevation of high-density lipoproteins and gender-specific alterations of lipid metabolism
    • 10.1371/journal.pone.0058856
    • O. Beaslas, J. Metso, E. Nissilä, P.P. Laurila, E. Kaiharju, and K.C. Batchu Osbpl8 deficiency in mouse causes an elevation of high-density lipoproteins and gender-specific alterations of lipid metabolism PLoS One 8 2013 e58856 10.1371/journal.pone.0058856
    • (2013) PLoS One , vol.8 , pp. 58856
    • Beaslas, O.1    Metso, J.2    Nissilä, E.3    Laurila, P.P.4    Kaiharju, E.5    Batchu, K.C.6
  • 115
    • 70349263990 scopus 로고    scopus 로고
    • OSBPL10, a novel candidate gene for high triglyceride trait in dyslipidemic Finnish subjects, regulates cellular lipid metabolism
    • J. Perttilä, K. Merikanto, J. Naukkarinen, I. Surakka, N.W. Martin, and K. Tanhuanpää OSBPL10, a novel candidate gene for high triglyceride trait in dyslipidemic Finnish subjects, regulates cellular lipid metabolism J Mol Med (Berl) 87 2009 825 835
    • (2009) J Mol Med (Berl) , vol.87 , pp. 825-835
    • Perttilä, J.1    Merikanto, K.2    Naukkarinen, J.3    Surakka, I.4    Martin, N.W.5    Tanhuanpää, K.6
  • 117
    • 78249283533 scopus 로고    scopus 로고
    • Identification of evidence suggestive of an association with peripheral arterial disease at the OSBPL10 locus by genome-wide investigation in the Japanese population
    • H. Koriyama, H. Nakagami, T. Katsuya, K. Sugimoto, H. Yamashita, and Y. Takami Identification of evidence suggestive of an association with peripheral arterial disease at the OSBPL10 locus by genome-wide investigation in the Japanese population J Atheroscler Thromb 17 2010 1054 1062
    • (2010) J Atheroscler Thromb , vol.17 , pp. 1054-1062
    • Koriyama, H.1    Nakagami, H.2    Katsuya, T.3    Sugimoto, K.4    Yamashita, H.5    Takami, Y.6
  • 119
    • 75649087405 scopus 로고    scopus 로고
    • Differential epigenomic and transcriptomic responses in subcutaneous adipose tissue between low and high responders to caloric restriction
    • L. Bouchard, R. Rabasa-Lhoret, M. Faraj, M.E. Lavoie, J. Mill, and L. Perusse Differential epigenomic and transcriptomic responses in subcutaneous adipose tissue between low and high responders to caloric restriction Am J Clin Nutr 91 2010 309 320
    • (2010) Am J Clin Nutr , vol.91 , pp. 309-320
    • Bouchard, L.1    Rabasa-Lhoret, R.2    Faraj, M.3    Lavoie, M.E.4    Mill, J.5    Perusse, L.6
  • 120
    • 77958092090 scopus 로고    scopus 로고
    • OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the Golgi-late endosome interface
    • Y. Zhou, S. Li, M.I. Mäyränpää, W. Zhong, N. Back, and D. Yan OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the Golgi-late endosome interface Exp Cell Res 316 2010 3304 3316
    • (2010) Exp Cell Res , vol.316 , pp. 3304-3316
    • Zhou, Y.1    Li, S.2    Mäyränpää, M.I.3    Zhong, W.4    Back, N.5    Yan, D.6
  • 121
    • 84875167919 scopus 로고    scopus 로고
    • CAMP-stimulated phosphorylation of diaphanous 1 regulates protein stability and interaction with binding partners in adrenocortical cells
    • D. Li, E.B. Dammer, N.C. Lucki, and M.B. Sewer CAMP-stimulated phosphorylation of diaphanous 1 regulates protein stability and interaction with binding partners in adrenocortical cells Mol Biol Cell 24 2013 848 857
    • (2013) Mol Biol Cell , vol.24 , pp. 848-857
    • Li, D.1    Dammer, E.B.2    Lucki, N.C.3    Sewer, M.B.4
  • 122
    • 0028213802 scopus 로고
    • A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein
    • B. Jiang, J.L. Brown, J. Sheraton, N. Fortin, and H. Bussey A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein Yeast 10 1994 341 353
    • (1994) Yeast , vol.10 , pp. 341-353
    • Jiang, B.1    Brown, J.L.2    Sheraton, J.3    Fortin, N.4    Bussey, H.5
  • 123
    • 0028048619 scopus 로고
    • SWH1 from yeast encodes a candidate nuclear factor containing ankyrin repeats and showing homology to mammalian oxysterol-binding protein
    • W.A. Schmalix, and W. Bandlow SWH1 from yeast encodes a candidate nuclear factor containing ankyrin repeats and showing homology to mammalian oxysterol-binding protein Biochim Biophys Acta 1219 1994 205 210
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 205-210
    • Schmalix, W.A.1    Bandlow, W.2
  • 124
    • 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
    • X. Li, M.P. Rivas, M. Fang, J. Marchena, B. Mehrotra, and A. Chaudhary Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex J Cell Biol 157 2002 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
  • 125
    • 34848818827 scopus 로고    scopus 로고
    • The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function
    • G.D. Fairn, A.J. Curwin, C.J. Stefan, and C.R. McMaster The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function Proc Natl Acad Sci USA 104 2007 15352 15357
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15352-15357
    • Fairn, G.D.1    Curwin, A.J.2    Stefan, C.J.3    McMaster, C.R.4
  • 126
    • 77958519249 scopus 로고    scopus 로고
    • Lipid binding requirements for oxysterol-binding protein Kes1 inhibition of autophagy and endosome-trans-Golgi trafficking pathways
    • M.A. LeBlanc, and C.R. McMaster Lipid binding requirements for oxysterol-binding protein Kes1 inhibition of autophagy and endosome-trans-Golgi trafficking pathways J Biol Chem 285 2010 33875 33884
    • (2010) J Biol Chem , vol.285 , pp. 33875-33884
    • Leblanc, M.A.1    McMaster, C.R.2
  • 127
    • 84883453530 scopus 로고    scopus 로고
    • Insights into the mechanisms of sterol transport between organelles
    • [Epub ahead of print] PMID: 23283302
    • B. Mesmin, B. Antonny, and G. Drin Insights into the mechanisms of sterol transport between organelles Cell Mol Life Sci Jan 3 2013 [Epub ahead of print] PMID: 23283302
    • (2013) Cell Mol Life Sci , Issue.JAN 3
    • Mesmin, B.1    Antonny, B.2    Drin, G.3
  • 128
    • 33746939368 scopus 로고    scopus 로고
    • Homologues of Oxysterol-Binding Proteins Affect Cdc42p- and Rho1p-Mediated Cell Polarization in Saccharomyces cerevisiae
    • K.G. Kozminski, G. Alfaro, S. Dighe, and C.T. Beh Homologues of Oxysterol-Binding Proteins Affect Cdc42p- and Rho1p-Mediated Cell Polarization in Saccharomyces cerevisiae Traffic 7 2006 1224 1242
    • (2006) Traffic , vol.7 , pp. 1224-1242
    • Kozminski, K.G.1    Alfaro, G.2    Dighe, S.3    Beh, C.T.4
  • 129
    • 33947398366 scopus 로고    scopus 로고
    • Central roles of small GTPases in the development of cell polarity in yeast and beyond
    • H.O. Park, and E. Bi Central roles of small GTPases in the development of cell polarity in yeast and beyond Microbiol Mol Biol Rev 71 2007 48 96
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 48-96
    • Park, H.O.1    Bi, E.2
  • 131
    • 84857283848 scopus 로고    scopus 로고
    • A sterol-binding protein integrates endosomal lipid metabolism with TOR signaling and nitrogen sensing
    • C.J. Mousley, P. Yuan, N.A. Gaur, K.D. Trettin, A.H. Nile, and S.J. Deminoff A sterol-binding protein integrates endosomal lipid metabolism with TOR signaling and nitrogen sensing Cell 148 2012 702 715
    • (2012) Cell , vol.148 , pp. 702-715
    • Mousley, C.J.1    Yuan, P.2    Gaur, N.A.3    Trettin, K.D.4    Nile, A.H.5    Deminoff, S.J.6
  • 132
    • 84875942257 scopus 로고    scopus 로고
    • The yeast oxysterol binding protein kes1 maintains sphingolipid levels
    • 10.1371/journal.pone.0060485
    • M.A. Leblanc, G.D. Fairn, S.B. Russo, O. Czyz, V. Zaremberg, and L.A. Cowart The yeast oxysterol binding protein kes1 maintains sphingolipid levels PLoS One 8 4 2013 e60485 10.1371/journal.pone.0060485
    • (2013) PLoS One , vol.8 , Issue.4 , pp. 60485
    • Leblanc, M.A.1    Fairn, G.D.2    Russo, S.B.3    Czyz, O.4    Zaremberg, V.5    Cowart, L.A.6
  • 133
    • 84861881131 scopus 로고    scopus 로고
    • Osh6 overexpression extends the lifespan of yeast by increasing vacuole fusion
    • S. Gebre, R. Connor, Y. Xia, S. Jawed, J.M. Bush, and M. Bard Osh6 overexpression extends the lifespan of yeast by increasing vacuole fusion Cell Cycle 11 2012 2176 2188
    • (2012) Cell Cycle , vol.11 , pp. 2176-2188
    • Gebre, S.1    Connor, R.2    Xia, Y.3    Jawed, S.4    Bush, J.M.5    Bard, M.6
  • 134
    • 25444460845 scopus 로고    scopus 로고
    • Molecular characterization of Osh6p, an oxysterol binding protein homolog in the yeast Saccharomyces cerevisiae
    • P. Wang, W. Duan, A.L. Munn, and H. Yang Molecular characterization of Osh6p, an oxysterol binding protein homolog in the yeast Saccharomyces cerevisiae FEBS J 272 2005 4703 4715
    • (2005) FEBS J , vol.272 , pp. 4703-4715
    • Wang, P.1    Duan, W.2    Munn, A.L.3    Yang, H.4
  • 135
    • 25444529050 scopus 로고    scopus 로고
    • AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism
    • P. Wang, Y. Zhang, H. Li, H.K. Chieu, A.L. Munn, and H. Yang AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism EMBO J 24 2005 2989 2999
    • (2005) EMBO J , vol.24 , pp. 2989-2999
    • Wang, P.1    Zhang, Y.2    Li, H.3    Chieu, H.K.4    Munn, A.L.5    Yang, H.6
  • 136
    • 84870793680 scopus 로고    scopus 로고
    • ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology
    • A.G. Manford, C.J. Stefan, H.L. Yuan, J.A. Macgurn, and S.D. Emr ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology Dev Cell 23 2012 1129 1140
    • (2012) Dev Cell , vol.23 , pp. 1129-1140
    • Manford, A.G.1    Stefan, C.J.2    Yuan, H.L.3    Macgurn, J.A.4    Emr, S.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.