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Volumn 310, Issue 2, 2005, Pages 445-462

Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; ISOENZYME; ISOPROTEIN; LIGAND; LIPID; OXYSTEROL BINDING PROTEIN RELATED PROTEIN 3; PEPTIDE DERIVATIVE; PHENYLALANYLPHENYLALANYLALANYLTHREONINE; PHOSPHATIDYLINOSITOL 3 KINASE; PLECKSTRIN; UNCLASSIFIED DRUG; VAMP ASSOCIATED PROTEIN A;

EID: 26844518949     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.08.003     Document Type: Article
Times cited : (75)

References (48)
  • 2
    • 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. Rodriquez 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    Rodriquez, I.R.5
  • 3
    • 0037455984 scopus 로고    scopus 로고
    • The OSBP-related proteins: A novel protein family involved in vesicle transport, cellular lipid metabolism, and cell signaling
    • M. Lehto, and V.M. Olkkonen The OSBP-related proteins: a novel protein family involved in vesicle transport, cellular lipid metabolism, and cell signaling Biochim. Biophys. Acta 1631 2003 1 11
    • (2003) Biochim. Biophys. Acta , vol.1631 , pp. 1-11
    • Lehto, M.1    Olkkonen, V.M.2
  • 4
    • 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
  • 5
    • 0019809230 scopus 로고
    • Assay of oxysterol-binding protein in a mouse fibroblast, a cell free system
    • A.A. Kandutsch, and E.P. Shown Assay of oxysterol-binding protein in a mouse fibroblast, a cell free system J. Biol. Chem. 256 1981 13068 13073
    • (1981) J. Biol. Chem. , vol.256 , pp. 13068-13073
    • Kandutsch, A.A.1    Shown, E.P.2
  • 7
    • 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
  • 8
    • 0035947666 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina
    • E.F. Moreira, C. Jaworski, A. Li, and I.R. Rodriquez Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina J. Biol. Chem. 276 2001 18570 18578
    • (2001) J. Biol. Chem. , vol.276 , pp. 18570-18578
    • Moreira, E.F.1    Jaworski, C.2    Li, A.3    Rodriquez, I.R.4
  • 9
    • 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
  • 10
    • 0035947559 scopus 로고    scopus 로고
    • Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport
    • Y. Xu, Y. Liu, N.D. Ridgway, and C.R. McMaster Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport J. Biol. Chem. 276 2001 18407 18414
    • (2001) J. Biol. Chem. , vol.276 , pp. 18407-18414
    • Xu, Y.1    Liu, Y.2    Ridgway, N.D.3    McMaster, C.R.4
  • 11
    • 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. Mehrotha, A. Chaudhary, L. Feng, G.D. Prestwich, and V.A. Bankaitis 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    Mehrotha, B.5    Chaudhary, A.6    Feng, L.7    Prestwich, G.D.8    Bankaitis, V.A.9
  • 12
    • 18844430347 scopus 로고    scopus 로고
    • Identification and assessment the role of a nominal phospholipids binding region of oxysterol binding protein ORP1S in the regulation of vesicular transport
    • G.D. Fairn, and C.R. McMaster Identification and assessment the role of a nominal phospholipids binding region of oxysterol binding protein ORP1S 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
  • 15
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • M.A. Lemmon, and K.M. Ferguson Signal-dependent membrane targeting by pleckstrin homology (PH) domains Biochem. J. 350 2000 1 18
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 17
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components
    • T.P. Levine, and S. Munro Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components Curr. Biol. 12 2002 695 704
    • (2002) Curr. Biol. , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 18
    • 7244248722 scopus 로고    scopus 로고
    • Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p
    • A. Roy, and T.P. Levine Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p J. Biol. Chem. 279 2004 44683 44689
    • (2004) J. Biol. Chem. , vol.279 , pp. 44683-44689
    • Roy, A.1    Levine, T.P.2
  • 19
    • 0033534788 scopus 로고    scopus 로고
    • Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins
    • Y. Nishimura, M. Hayashi, H. Inada, and T. Tanaka Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins Biochem. Biophys. Res. Commun. 254 1999 21 26
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 21-26
    • Nishimura, Y.1    Hayashi, M.2    Inada, H.3    Tanaka, T.4
  • 20
    • 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
    • J.P Wyles, C.R. McMaster, and N.D. Ridgway 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 2002 29908 29918
    • (2002) J. Biol. Chem. , vol.277 , pp. 29908-29918
    • Wyles, J.P.1    McMaster, C.R.2    Ridgway, N.D.3
  • 21
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • C.J.R. 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.R.1    Roy, A.2    Levine, T.P.3
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin homology domain of oxysterol binding protein recognizes a determinant specific to Golgi membranes
    • T.P. Levine, and S. Munro The pleckstrin homology domain of oxysterol binding protein recognizes 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
  • 26
    • 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
  • 28
    • 20444402239 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of ceramide transport
    • R.J. Perry, and N.D. Ridgway Molecular mechanisms and regulation of ceramide transport Biochim. Biophys. Acta 1734 2005 220 234
    • (2005) Biochim. Biophys. Acta , vol.1734 , pp. 220-234
    • Perry, R.J.1    Ridgway, N.D.2
  • 29
    • 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
    • T.A. Lagace, D.M. Byers, H.W. Cook, and N.D. Ridgway 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 1997 205 213
    • (1997) Biochem. J. , vol.326 , pp. 205-213
    • Lagace, T.A.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 30
    • 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
  • 33
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of low-density lipoprotein in cultured cells
    • J.L. Goldstein, S.K. Basu, and M.S. Brown Receptor-mediated endocytosis of low-density lipoprotein in cultured cells Methods Enzymol. 98 1983 241 260
    • (1983) Methods Enzymol. , vol.98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 34
    • 0029825831 scopus 로고    scopus 로고
    • Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin
    • G. Schiavo, Q.M. Gu, G.D. Prestwich, T.H. Söllner, and J.E. Rothman Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin Proc. Natl. Acad. Sci. 93 1996 13327 13332
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13327-13332
    • Schiavo, G.1    Gu, Q.M.2    Prestwich, G.D.3    Söllner, T.H.4    Rothman, J.E.5
  • 35
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • S.G. Rhee Regulation of phosphoinositide-specific phospholipase C Annu. Rev. Biochem. 70 2001 281 312
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 37
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in mammalian cells
    • E.-L. Eskelinen Maturation of autophagic vacuoles in mammalian cells Autophagy 1 2005 1 10
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.-L.1
  • 38
    • 0032869187 scopus 로고    scopus 로고
    • The role of the 3-hydroxy 3-methylglutaryl coenzyme a reductase cytosolic domain in karmellae biogenesis
    • D.A. Profant, C.J. Roberts, A.J. Koning, and R.L. Wright The role of the 3-hydroxy 3-methylglutaryl coenzyme A reductase cytosolic domain in karmellae biogenesis Mol. Biol. Cell 10 1999 3409 3423
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3409-3423
    • Profant, D.A.1    Roberts, C.J.2    Koning, A.J.3    Wright, R.L.4
  • 39
    • 14044268935 scopus 로고    scopus 로고
    • Differential regulation of ER structure though VAP-Nir protein interaction
    • R. Amarilio, S. Rmachandran, H. Sabanay, and S. Lev Differential regulation of ER structure though VAP-Nir protein interaction J. Biol. Chem. 280 2005 5934 5944
    • (2005) J. Biol. Chem. , vol.280 , pp. 5934-5944
    • Amarilio, R.1    Rmachandran, S.2    Sabanay, H.3    Lev, S.4
  • 41
    • 0032498627 scopus 로고    scopus 로고
    • A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolization of the endoplasmic reticulum
    • L. Abrami, M. Fivaz, P.-E. Glauser, R.G. Parton, and F.G. van der Goot A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolization of the endoplasmic reticulum J. Cell Biol. 140 1998 525 540
    • (1998) J. Cell Biol. , vol.140 , pp. 525-540
    • Abrami, L.1    Fivaz, M.2    Glauser, P.-E.3    Parton, R.G.4    Van Der Goot, F.G.5
  • 42
    • 0033567854 scopus 로고    scopus 로고
    • Toxicity of tunicamycin to cultured brain neurons: Ultrastructure of the degenerating neurons
    • T.Y. Lin, S.M. Wang, W.M. Fu, Y.H. Chen, and H.S. Yin Toxicity of tunicamycin to cultured brain neurons: ultrastructure of the degenerating neurons J. Cell. Biochem. 74 1999 638 647
    • (1999) J. Cell. Biochem. , vol.74 , pp. 638-647
    • Lin, T.Y.1    Wang, S.M.2    Fu, W.M.3    Chen, Y.H.4    Yin, H.S.5
  • 43
    • 0032942210 scopus 로고    scopus 로고
    • Brefeldin a (BFA) disrupts the organization of the microtubule and the actin cytoskeletons
    • C. Alvarez, and E.S. Sztul Brefeldin A (BFA) disrupts the organization of the microtubule and the actin cytoskeletons Eur. J. Cell Biol. 78 1999 1 14
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 1-14
    • Alvarez, C.1    Sztul, E.S.2
  • 44
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • S. Dalal, M.F.N. Rosser, D.M. Cyr, and P.I. Hanson Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway Mol. Biol. Cell 15 2004 637 648
    • (2004) Mol. Biol. Cell , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.N.2    Cyr, D.M.3    Hanson, P.I.4
  • 46
    • 0026746713 scopus 로고
    • Inhibition by brefeldin a of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • J.B. Helms, and J.E. Rothman Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF Nature 369 1992 352 354
    • (1992) Nature , vol.369 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 47
    • 0033950864 scopus 로고    scopus 로고
    • Turning of ARF; The Sec7 family of guanine-nucleotide-exchange factors
    • C.L. Jackson, and J.E. Casanova Turning of ARF; the Sec7 family of guanine-nucleotide-exchange factors Trends Cell Biol. 10 2000 60 67
    • (2000) Trends Cell Biol. , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 48
    • 0034947717 scopus 로고    scopus 로고
    • Golgi localization and phosphorylation of oxysterol binding protein in Niemann-Pick C and U18666-treated cells
    • A. Mohammadi, R.J. Perry, M.K. Storey, H.W. Cook, D.M. Byers, and N.D. Ridgway Golgi localization and phosphorylation of oxysterol binding protein in Niemann-Pick C and U18666-treated cells J. Lipid. Res. 42 2001 1062 1071
    • (2001) J. Lipid. Res. , vol.42 , pp. 1062-1071
    • Mohammadi, A.1    Perry, R.J.2    Storey, M.K.3    Cook, H.W.4    Byers, D.M.5    Ridgway, N.D.6


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