메뉴 건너뛰기




Volumn 2, Issue 1, 2007, Pages 85-94

OSBP-related proteins: Lipid sensors or transporters?

Author keywords

25 hydroxycholesterol; Cell signaling; Lipid metabolism; Lipid transport; Oxysterol binding protein; Oxysterol binding protein related proteins; Sterol sensor; Vesicle transport

Indexed keywords

BINDING PROTEIN; OXYSTEROL BINDING PROTEIN RELATED PROTEIN; SPHINGOMYELIN; UNCLASSIFIED DRUG;

EID: 34249285522     PISSN: 17460875     EISSN: None     Source Type: Journal    
DOI: 10.2217/17460875.2.1.85     Document Type: Review
Times cited : (10)

References (74)
  • 1
    • 0037455984 scopus 로고    scopus 로고
    • AThe OSBP-related proteins: A novel protein family involved in vesicle transport, cellular lipid metabolism, and cell signalling
    • Lehto M, Olkkonen VM:AThe OSBP-related proteins: a novel protein family involved in vesicle transport, cellular lipid metabolism, and cell signalling. Biochim. Biophys. Acta 1631, 1-11 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1631 , pp. 1-11
    • Lehto, M.1    Olkkonen, V.M.2
  • 2
    • 0035885867 scopus 로고    scopus 로고
    • A family of 12 human genes containing oxysterol-binding domains
    • Jaworski CJ, Moreira E, Li A et al.: A family of 12 human genes containing oxysterol-binding domains. Genomics 78, 185-196 (2001).
    • (2001) Genomics , vol.78 , pp. 185-196
    • Jaworski, C.J.1    Moreira, E.2    Li, A.3
  • 3
    • 0034891766 scopus 로고    scopus 로고
    • The OSBP-related protein family in humans
    • Lehto M, Laitinen S, Chinetti G et al.: The OSBP-related protein family in humans. J. Lipid Res. 42, 1203-1213 (2001).
    • (2001) J. Lipid Res , vol.42 , pp. 1203-1213
    • Lehto, M.1    Laitinen, S.2    Chinetti, G.3
  • 4
    • 0036375928 scopus 로고    scopus 로고
    • An oxysterol-binding protein family identified in the mouse
    • Anniss AM, Apostolopoulos J, Dworkin S et al.: An oxysterol-binding protein family identified in the mouse. DNA Cell Biol. 21, 571-580 (2002).
    • (2002) DNA Cell Biol , vol.21 , pp. 571-580
    • Anniss, A.M.1    Apostolopoulos, J.2    Dworkin, S.3
  • 5
    • 0037268726 scopus 로고    scopus 로고
    • ORP3 splice variants and their expression in human tissues and hematopoietic cells
    • Collier FM, Gregorio-King CC, Apostolopoulos J et al.: ORP3 splice variants and their expression in human tissues and hematopoietic cells. DNA Cell Biol. 22, 1-9 (2003).
    • (2003) DNA Cell Biol , vol.22 , pp. 1-9
    • Collier, F.M.1    Gregorio-King, C.C.2    Apostolopoulos, J.3
  • 6
    • 0032554080 scopus 로고    scopus 로고
    • A Drosophila homologue of oxysterol binding protein (OSBP) - implications for the role of OSBP
    • Alphey L, Jimenez J, Glover D: A Drosophila homologue of oxysterol binding protein (OSBP) - implications for the role of OSBP Biochim. Biophys. Acta 1395, 159-164 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1395 , pp. 159-164
    • Alphey, L.1    Jimenez, J.2    Glover, D.3
  • 7
    • 0034885330 scopus 로고    scopus 로고
    • BIP, a BRAM-interacting protein involved in TGF-β signalling, regulates body length in Caenorhabditis elegans
    • Sugawara K, Morita K, Ueno N, Shibuya H: BIP, a BRAM-interacting protein involved in TGF-β signalling, regulates body length in Caenorhabditis elegans. Genes Cells 6, 599-606 (2001).
    • (2001) Genes Cells , vol.6 , pp. 599-606
    • Sugawara, K.1    Morita, K.2    Ueno, N.3    Shibuya, H.4
  • 8
    • 0037063345 scopus 로고    scopus 로고
    • OSBPa, a predicted oxysterol binding protein of Dictyostellium, is required for regulated entry into culmination
    • Fukuzawa M, Williams JG: OSBPa, a predicted oxysterol binding protein of Dictyostellium, is required for regulated entry into culmination. FEBS Lett. 527, 37-42 (2002).
    • (2002) FEBS Lett , vol.527 , pp. 37-42
    • Fukuzawa, M.1    Williams, J.G.2
  • 9
    • 33745177734 scopus 로고    scopus 로고
    • Two distinct oxysterol binding protein-related proteins in the parasitic protist Cryptosporidium parvum (Apicomplexa)
    • Zeng B, Zhu G: Two distinct oxysterol binding protein-related proteins in the parasitic protist Cryptosporidium parvum (Apicomplexa). Biochem. Biophys. Res. Commun. 346, 591-599 (2006).
    • (2006) Biochem. Biophys. Res. Commun , vol.346 , pp. 591-599
    • Zeng, B.1    Zhu, G.2
  • 10
    • 0842323769 scopus 로고    scopus 로고
    • Potato oxysterol binding protein and cathepsin B are rapidly up-regulated in independent defence pathways that distinguish R gene-mediated and field resistences to Phytophthora infestans
    • Avrova AO, Nawsheen T, Rokka V-M et al.: Potato oxysterol binding protein and cathepsin B are rapidly up-regulated in independent defence pathways that distinguish R gene-mediated and field resistences to Phytophthora infestans. Mol. Plant Pathol. 5, 45-46 (2004).
    • (2004) Mol. Plant Pathol , vol.5 , pp. 45-46
    • Avrova, A.O.1    Nawsheen, T.2    Rokka, V.-M.3
  • 11
    • 33746786407 scopus 로고    scopus 로고
    • Identification and characterization of PiORP1, a Petunia oxysterol-binding-protein related protein involved in receptor-kinase mediated signaling in pollen, and analysis of the ORPgene family in Arabidopsis
    • Skirpan AL, Dowd PE, Sijacic P et al.: Identification and characterization of PiORP1, a Petunia oxysterol-binding-protein related protein involved in receptor-kinase mediated signaling in pollen, and analysis of the ORPgene family in Arabidopsis. Plant Mol. Biol. 61, 553-565 (2006).
    • (2006) Plant Mol. Biol , vol.61 , pp. 553-565
    • Skirpan, A.L.1    Dowd, P.E.2    Sijacic, P.3
  • 12
    • 0021747172 scopus 로고
    • Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
    • Taylor FR, Saucier SE, Shown EP et al.: Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase. J. Blol. Chem. 259, 12382-12387 (1984).
    • (1984) J. Blol. Chem , vol.259 , pp. 12382-12387
    • Taylor, F.R.1    Saucier, S.E.2    Shown, E.P.3
  • 13
    • 0024422669 scopus 로고
    • CDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper
    • Dawson PA, Ridgway ND, Slaughter CA, Brown MS, Goldstein JL: CDNA cloning and expression of oxysterol-binding protein, an oligomer with a potential leucine zipper. J. Biol. Chem. 264, 16798-16803 (1989).
    • (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
  • 15
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-retated proteins
    • Im YJ, Raychaudhuri S, Prinz WA, Hurley JH: Structural mechanism for sterol sensing and transport by OSBP-retated proteins. Nature 437, 154-158 (2005).
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 16
    • 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
    • Johansson M, Bocher V, Lehto M et al.: 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, 903-915 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 903-915
    • Johansson, M.1    Bocher, V.2    Lehto, M.3
  • 17
    • 0036188574 scopus 로고    scopus 로고
    • ORP2, a homolog of oxysterol binding protein, regulates cellular cholesterol metabolism
    • Laitinen S, Lehto M, Lehtonen S et al.: ORP2, a homolog of oxysterol binding protein, regulates cellular cholesterol metabolism. J. Lipid Res. 43, 245-255 (2002).
    • (2002) J. Lipid Res , vol.43 , pp. 245-255
    • Laitinen, S.1    Lehto, M.2    Lehtonen, S.3
  • 18
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes
    • Levine TP, Munro S: The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes. Curr. Biol. 8, 729-739 (1998).
    • (1998) Curr. Biol , vol.8 , pp. 729-739
    • Levine, T.P.1    Munro, S.2
  • 19
    • 0026564767 scopus 로고
    • Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding
    • Ridgway ND, Dawson PA, Ho YK et al.: Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding. J. Cell Biol. 116, 307-319 (1992).
    • (1992) J. Cell Biol , vol.116 , pp. 307-319
    • Ridgway, N.D.1    Dawson, P.A.2    Ho, Y.K.3
  • 20
    • 2342447668 scopus 로고    scopus 로고
    • Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: The expression and intracellular localization of ORP3, ORP6, and ORP7
    • Lehto M, Tienari J, Lehtonen S et al.: Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: The expression and intracellular localization of ORP3, ORP6, and ORP7. Cell Tissue Res. 315, 39-57 (2004).
    • (2004) Cell Tissue Res , vol.315 , pp. 39-57
    • Lehto, M.1    Tienari, J.2    Lehtonen, S.3
  • 21
    • 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
    • Wyles JP, Ridgway ND: VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus. Exp. Cell Res. 297, 533-547 (2004).
    • (2004) Exp. Cell Res , vol.297 , pp. 533-547
    • Wyles, J.P.1    Ridgway, N.D.2
  • 22
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    • Raychaudhuri S, Im YJ, Hurley JH, Prim WA: Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides. J. Cell Biol. 173, 107-119 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 107-119
    • Raychaudhuri, S.1    Im, Y.J.2    Hurley, J.H.3    Prim, W.A.4
  • 23
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • Loewen CJ, Roy A, Levine TP: 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.1    Roy, A.2    Levine, T.P.3
  • 24
    • 0030882949 scopus 로고    scopus 로고
    • Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain
    • Lagace TA, Byers DM, Cook HW, Ridgway ND: Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain. Biochem. J. 326, 205-213 (1997).
    • (1997) Biochem. J , vol.326 , pp. 205-213
    • Lagace, T.A.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 25
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components
    • Levine TP, Munro S: Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components. Curr. Biol. 12, 695-704 (2002).
    • (2002) Curr. Biol , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 26
    • 2342556630 scopus 로고    scopus 로고
    • FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P
    • Godi A, Di Campli A, Konstantakopoulos A et al.: FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat. Cell Biol. 6, 393-404 (2004).
    • (2004) Nat. Cell Biol , vol.6 , pp. 393-404
    • Godi, A.1    Di Campli, A.2    Konstantakopoulos, A.3
  • 27
    • 26844518949 scopus 로고    scopus 로고
    • Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants
    • Lehto M, Hynynen R, Karjalainen K et al.: Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants. Exp. Cell Res. 310, 445-462 (2005).
    • (2005) Exp. Cell Res , vol.310 , pp. 445-462
    • Lehto, M.1    Hynynen, R.2    Karjalainen, K.3
  • 28
    • 0347611095 scopus 로고    scopus 로고
    • Molecular machinery for non-vesicular trafficking of ceramide
    • Hanada K, Kumagai K, Yasuda S 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    Kumagai, K.2    Yasuda, S.3
  • 29
    • 14044268935 scopus 로고    scopus 로고
    • Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction
    • Amarillo R, Ramachandran S, Sabanay H, Lev S: Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction. J. Biol. Chem. 280, 5934-5944 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 5934-5944
    • Amarillo, R.1    Ramachandran, S.2    Sabanay, H.3    Lev, S.4
  • 30
    • 2942518361 scopus 로고    scopus 로고
    • The role of the Nir/rdgB protein family in membrane trafficking and cytoskeleton remodeling
    • Lev S: The role of the Nir/rdgB protein family in membrane trafficking and cytoskeleton remodeling. Exp. Cell Res. 297, 1-10 (2004).
    • (2004) Exp. Cell Res , vol.297 , pp. 1-10
    • Lev, S.1
  • 31
    • 2942677427 scopus 로고    scopus 로고
    • Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid
    • Loewen CJ, Gaspar ML, Jesch SA et al.: Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid. Science 304, 1644-1647 (2004).
    • (2004) Science , vol.304 , pp. 1644-1647
    • Loewen, C.J.1    Gaspar, M.L.2    Jesch, S.A.3
  • 32
    • 8744254603 scopus 로고    scopus 로고
    • Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae
    • Kvam E, Goldfarb DS: Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae. J. Cell Sci. 117, 4959-4968 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 4959-4968
    • Kvam, E.1    Goldfarb, D.S.2
  • 33
    • 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 TP, 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 12. 1633-1644 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 34
    • 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
  • 35
    • 2342637722 scopus 로고    scopus 로고
    • Oxysterol binding proteins: In more than one place at one time?
    • Olkkonen VM, Levine TPI Oxysterol binding proteins: in more than one place at one time? Biochem. Cell Biol. 82, 87-98 (2004).
    • (2004) Biochem. Cell Biol , vol.82 , pp. 87-98
    • Olkkonen, V.M.1    Levine, T.P.I.2
  • 36
    • 27744604253 scopus 로고    scopus 로고
    • Nonclassical PITPs activate PLD via the Stt4p PtdIns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast
    • Routt SM, Ryan MM, Tyeryar K et al.: Nonclassical PITPs activate PLD via the Stt4p PtdIns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast. Traffic 6, 1157-1172 (2005).
    • (2005) Traffic , vol.6 , pp. 1157-1172
    • Routt, S.M.1    Ryan, M.M.2    Tyeryar, K.3
  • 37
    • 0034947717 scopus 로고    scopus 로고
    • Golgi localization and phosphorylation of oxysterol binding protein in Niemann-Pick C and U18666A-treated cells
    • Mohammadi A, Perry RJ, Storey MK et al.: Golgi localization and phosphorylation of oxysterol binding protein in Niemann-Pick C and U18666A-treated cells. J. Lipid Res. 42, 1062-1071 (2001).
    • (2001) J. Lipid Res , vol.42 , pp. 1062-1071
    • Mohammadi, A.1    Perry, R.J.2    Storey, M.K.3
  • 38
    • 0032553324 scopus 로고    scopus 로고
    • Differential effects of sphingomyelin hydrolysis and cholesterol transport on oxysterol-binding protein phosphorylation and Golgi localization
    • Ridgway ND, Lagace TA, Cook HW, Byers DM: Differential effects of sphingomyelin hydrolysis and cholesterol transport on oxysterol-binding protein phosphorylation and Golgi localization. J. Biol. Chem. 273, 31621-31628 (1998).
    • (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
  • 39
    • 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
    • Storey MK, Byers DM, Cook HW, Ridgway ND: 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, 247-256 (1998).
    • (1998) Biochem. J , vol.336 , pp. 247-256
    • Storey, M.K.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 40
    • 23844453427 scopus 로고    scopus 로고
    • Inhibition of cholesterol biosynthesis by 25-hydroxycholesterol is independent of OSBP
    • Nishimura T, Inoue T, Shibata N et al.: Inhibition of cholesterol biosynthesis by 25-hydroxycholesterol is independent of OSBP, Genes Cells 10, 793-801 (2005).
    • (2005) Genes Cells , vol.10 , pp. 793-801
    • Nishimura, T.1    Inoue, T.2    Shibata, N.3
  • 41
    • 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
    • Lagace TA, Byers DM, Cook HW, Ridgway ND: Chinese hamster ovary cells overexpressing the oxysterol binding protein (OSBP) display enhanced synthesis of sphingomyelin in response to 25-hydroxycholesterol. J. Lipid Res. 40, 109-116 (1999).
    • (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
  • 42
    • 0037119364 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum
    • Wyles JP, McMaster CR, Ridgway ND: Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum. J. Biol. Chem. 277, 29908-29918 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 29908-29918
    • Wyles, J.P.1    McMaster, C.R.2    Ridgway, N.D.3
  • 43
    • 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
    • Perry RJ, Ridgway ND: 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, 2604-2616 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2604-2616
    • Perry, R.J.1    Ridgway, N.D.2
  • 44
    • 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
  • 45
    • 20444402239 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of ceramide transport
    • Perry RJ, Ridgway ND: Molecular mechanisms and regulation of ceramide transport. Biochim. Biophys. Acta 1734, 220-234 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1734 , pp. 220-234
    • Perry, R.J.1    Ridgway, N.D.2
  • 46
    • 14644391519 scopus 로고    scopus 로고
    • OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation
    • Wang PY, Weng J, Anderson RG: OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation. Science 307, 1472-6 (2005).
    • (2005) Science , vol.307 , pp. 1472-1476
    • Wang, P.Y.1    Weng, J.2    Anderson, R.G.3
  • 47
    • 33845698910 scopus 로고    scopus 로고
    • Oxysterol binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation
    • Lessmann E, Ngo M, Leitges M et al.: Oxysterol binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation. Cell. Signal. 19, 384-392 (2007)
    • (2007) Cell. Signal , vol.19 , pp. 384-392
    • Lessmann, E.1    Ngo, M.2    Leitges, M.3
  • 48
    • 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 ND: Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments. Biochem. J. 361, 461-472 (2002).
    • (2002) Biochem. J , vol.361 , pp. 461-472
    • Wang, C.1    JeBailey, L.2    Ridgway, N.D.3
  • 49
    • 0035947666 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina
    • Moreira EF, Jaworski C, Li A, Rodriguez IR: Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina. J. Biol. Chem. 276, 18570-18578 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 18570-18578
    • Moreira, E.F.1    Jaworski, C.2    Li, A.3    Rodriguez, I.R.4
  • 50
    • 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, Tanhuanpaa K et al.: The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol. Biol. Cell 16, 5480-5492 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpaa, K.3
  • 51
    • 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
    • Fairn GD, McMaster CR: 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, 889-896 (2005).
    • (2005) Biochem. J , vol.387 , pp. 889-896
    • Fairn, G.D.1    McMaster, C.R.2
  • 52
    • 0035947559 scopus 로고    scopus 로고
    • Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport
    • Xu Y, Liu Y, Ridgway ND, McMaster CR: Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport. J. Biol. Chem. 276, 18407-18414 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 18407-18414
    • Xu, Y.1    Liu, Y.2    Ridgway, N.D.3    McMaster, C.R.4
  • 53
    • 23944475081 scopus 로고    scopus 로고
    • Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis
    • Hynynen R, Laitinen S, Käkelä R et al.: Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis. Biochem. J. 390, 273-283 (2005).
    • (2005) Biochem. J , vol.390 , pp. 273-283
    • Hynynen, R.1    Laitinen, S.2    Käkelä, R.3
  • 54
    • 23944462533 scopus 로고    scopus 로고
    • Overexpression of OSBP-related protein 2 (ORP2) in CHO cells induces alterations of phospholipid species composition
    • Käkelä R, Tanhuanpaa K, Laitinen S et al.: Overexpression of OSBP-related protein 2 (ORP2) in CHO cells induces alterations of phospholipid species composition. Biochem. Cell Biol. 83, 677-683 (2005).
    • (2005) Biochem. Cell Biol , vol.83 , pp. 677-683
    • Käkelä, R.1    Tanhuanpaa, K.2    Laitinen, S.3
  • 56
    • 10644239801 scopus 로고    scopus 로고
    • Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs
    • Adams CM, Reitz J, De Brabander JK et al.: Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs. J. Biol. Chem. 279, 52772-52780 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 52772-52780
    • Adams, C.M.1    Reitz, J.2    De Brabander, J.K.3
  • 57
    • 0037503924 scopus 로고    scopus 로고
    • Liver X receptor signaling pathways in cardiovascular disease
    • Tontonoz P, Mangelsdorf DJ: Liver X receptor signaling pathways in cardiovascular disease. Mol. Endocrinol. 17, 985-993 (2003).
    • (2003) Mol. Endocrinol , vol.17 , pp. 985-993
    • Tontonoz, P.1    Mangelsdorf, D.J.2
  • 58
    • 0028213802 scopus 로고
    • A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein
    • Jiang B, Brown JL, Sheraton J et al.: A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein. Yeast 10, 341-353 (1994).
    • (1994) Yeast , vol.10 , pp. 341-353
    • Jiang, B.1    Brown, J.L.2    Sheraton, J.3
  • 59
    • 0035108917 scopus 로고    scopus 로고
    • Overlapping functions of the yeast oxysterol-binding protein homologues
    • Beh CT, Cool L, Phillips J, Rine J: Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 157, 1117-1140 (2001).
    • (2001) Genetics , vol.157 , pp. 1117-1140
    • Beh, C.T.1    Cool, L.2    Phillips, J.3    Rine, J.4
  • 60
    • 4344641314 scopus 로고    scopus 로고
    • A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution
    • Beh CT, Rine J: A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution. J. Cell Sci. 117, 2983-2996 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 2983-2996
    • Beh, C.T.1    Rine, J.2
  • 61
    • 25444529050 scopus 로고    scopus 로고
    • AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism
    • Wang P, Zhang Y, Li H et al.: AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism. EMBO J. 24, 2989-2999 (2005).
    • (2005) EMBO J , vol.24 , pp. 2989-2999
    • Wang, P.1    Zhang, Y.2    Li, H.3
  • 62
    • 0029803610 scopus 로고    scopus 로고
    • Kes 1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis
    • Fang M, Kearns BG, Gedvilaite A et al.: Kes 1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. EMBO J. 15, 6447-6459 (1996).
    • (1996) EMBO J , vol.15 , pp. 6447-6459
    • Fang, M.1    Kearns, B.G.2    Gedvilaite, A.3
  • 63
    • 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 MP, Fang M et al.: Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. J. Cell Biol. 157, 63-77 (2002).
    • (2002) J. Cell Biol , vol.157 , pp. 63-77
    • Li, X.1    Rivas, M.P.2    Fang, M.3
  • 64
    • 28444461398 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae
    • Bankaitis VA, Phillips S, Yanagisawa L et al.: Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae. Adv. Enzyme Regul. 45, 155-170 (2005).
    • (2005) Adv. Enzyme Regul , vol.45 , pp. 155-170
    • Bankaitis, V.A.1    Phillips, S.2    Yanagisawa, L.3
  • 65
    • 33746939368 scopus 로고    scopus 로고
    • Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae
    • Kozminski KG, Alfaro, G, Dighe S, Beh CT: Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae, Traffic 7, 1224-1242 (2006).
    • (2006) Traffic , vol.7 , pp. 1224-1242
    • Kozminski, K.G.1    Alfaro, G.2    Dighe, S.3    Beh, C.T.4
  • 66
    • 0036791574 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Maxfield FR, Wustner D: Intracellular cholesterol transport. J. Clin. Invest. 110, 891-898 (2002).
    • (2002) J. Clin. Invest , vol.110 , pp. 891-898
    • Maxfield, F.R.1    Wustner, D.2
  • 68
    • 23744478870 scopus 로고    scopus 로고
    • Give lipids a START: The StAR-related lipid transfer (START) domain in mammals
    • Alpy F, TomasetTo C: Give lipids a START: the StAR-related lipid transfer (START) domain in mammals. J. Cell Sci. 118, 2791-2801 (2005).
    • (2005) J. Cell Sci , vol.118 , pp. 2791-2801
    • Alpy, F.1    TomasetTo, C.2
  • 69
    • 0347481137 scopus 로고    scopus 로고
    • Sterol carrier protein-2 selectively alters lipid composition and cholesterol dynamics of caveolae/lipid raft vs nonraft domains in L-cell fibroblast plasma membranes
    • Atshaves BP, Gallegos AM, McIntosh AL et al.: Sterol carrier protein-2 selectively alters lipid composition and cholesterol dynamics of caveolae/lipid raft vs nonraft domains in L-cell fibroblast plasma membranes. Biochemistry 42, 14583-14598 (2003).
    • (2003) Biochemistry , vol.42 , pp. 14583-14598
    • Atshaves, B.P.1    Gallegos, A.M.2    McIntosh, A.L.3
  • 70
    • 0029101538 scopus 로고
    • Sterol carrier protein-2 is involved in cholesterol transfer from the endoplasmic reticulum to the plasma membrane in human fibroblasts
    • Puglielli L, Rigotti A, Greco AV et al.: Sterol carrier protein-2 is involved in cholesterol transfer from the endoplasmic reticulum to the plasma membrane in human fibroblasts. J. Biol. Chem. 270, 18723-18726 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 18723-18726
    • Puglielli, L.1    Rigotti, A.2    Greco, A.V.3
  • 71
    • 4744363666 scopus 로고    scopus 로고
    • Sterol carrier protein-2-facilitated intermembrane transfer of cholesterol- and phospholipid-derived hydroperoxides
    • Vila A, Levchenko VV, Korytowski W, Girotti AW: Sterol carrier protein-2-facilitated intermembrane transfer of cholesterol- and phospholipid-derived hydroperoxides. Biochemistry 43, 12592-12605 (2004).
    • (2004) Biochemistry , vol.43 , pp. 12592-12605
    • Vila, A.1    Levchenko, V.V.2    Korytowski, W.3    Girotti, A.W.4
  • 72
    • 1542618335 scopus 로고    scopus 로고
    • Annexin 2-caveolin 1 complex is a target of ezetimibe and regulates intestinal cholesterol transport
    • Smart EJ, De Rose RA, Farber SA: Annexin 2-caveolin 1 complex is a target of ezetimibe and regulates intestinal cholesterol transport. Proc. Natl Acad. Sci. USA 101, 3450-3455 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3450-3455
    • Smart, E.J.1    De Rose, R.A.2    Farber, S.A.3
  • 73
    • 0037085452 scopus 로고    scopus 로고
    • Cholesteryl ester is transported from caveolae to internal membranes as part of a caveolin-annexin II lipid-protein complex
    • Uittenbogaard A, Everson WV, Matveev SV, Smart EJ: Cholesteryl ester is transported from caveolae to internal membranes as part of a caveolin-annexin II lipid-protein complex. J. Biol. Chem. 277, 4925-4931 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 4925-4931
    • Uittenbogaard, A.1    Everson, W.V.2    Matveev, S.V.3    Smart, E.J.4
  • 74
    • 0032513038 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking
    • Uittenbogaard A, Ying Y, Smart EJ: Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking. J. Biol. Chem. 273, 6525-6532 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 6525-6532
    • Uittenbogaard, A.1    Ying, Y.2    Smart, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.