341
Views
10
CrossRef citations to date
0
Altmetric
Reviews

OSBP-related proteins: lipid sensors or transporters?

&
Pages 85-94 | Published online: 18 Jan 2017

Bibliography

  • Lehto M, Olkkonen VM: The OSBP-related proteins: a novel protein family involved in vesicle transport, cellular lipid metabolism, and cell signalling. Biochim. Biophys. Acta 1631, 1–11 (2003).
  • Jaworski CJ, Moreira E, Li A et al.: A family of 12 human genes containing oxysterolbinding domains. Genomics 78, 185–196 (2001).
  • Lehto M, Laitinen S, Chinetti G et al.: The OSBP-related protein family in humans. J. Lipid Res. 42, 1203–1213 (2001).
  • Anniss AM, Apostolopoulos J, Dworkin S et al.: An oxysterol-binding protein family identified in the mouse. DNA Cell Biol. 21, 571–580 (2002).
  • 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).
  • 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).
  • Sugawara K, Morita K, Ueno N, Shibuya H: BIP, a BRAM-interacting protein involved in TGF- signalling, regulates body length in Caenorhabditis elegans. Genes Cells 6, 599–606 (2001).
  • Fukuzawa M, Williams JG: OSBPa, a predicted oxysterol binding protein of Dictyostelium, is required for regulated entry into culmination. FEBS Lett. 527, 37–42 (2002).
  • 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).
  • 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).
  • 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 ORP gene family in Arabidopsis. Plant Mol. Biol. 61, 553–565 (2006).
  • 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. Biol. Chem. 259, 12382–12387 (1984).
  • 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).
  • Dawson PA, Van der Westhuyzen DR, Goldstein JL, Brown MS: Purification of oxysterol binding protein from hamster liver cytosol. J. Biol. Chem. 264, 9046–9052 (1989).
  • Im YJ, Raychaudhuri S, Prinz WA, Hurley JH: Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437, 154–158 (2005).
  • Reports the first high-resolution structure of an oxysterol-bind ing protein (OSBP)- related protein (ORP), Saccharomyces cerevisiae Osh4p, revealing a pocket capable of accommodating a variety of sterols.
  • 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).
  • 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).
  • 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).
  • 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).
  • Lehto M, Tienari J, Lehtonen S et al.: Subfamily III of mammalian oxysterolbinding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7. Cell Tissue Res. 315, 39–57 (2004).
  • Wyles JP, Ridgway ND: VAMP-associated protein-A regulates partitioning of oxysterolbinding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus. Exp. Cell Res. 297, 533–547 (2004).
  • Raychaudhuri S, Im YJ, Hurley JH, PrinzWA: Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides. J. Cell Biol. 173, 107–119 (2006).
  • Provides the first direct evidence for the function of yeast ORPs as intracellular sterol transporters.
  • 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).
  • Identifies a mechanism by which ORPs and other proteins involved in lipid metabolism associate peripherally with the endoplasmic reticulum.
  • 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).
  • Levine TP, Munro S: Targeting of Golgispecific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components. Curr. Biol. 12, 695–704 (2002).
  • 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).
  • 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).
  • Hanada K, Kumagai K, Yasuda S et al.: Molecular machinery for non-vesicular trafficking of ceramide. Nature 426, 803–809 (2003).
  • Amarilio 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).
  • Lev S: The role of the Nir/rdgB protein family in membrane trafficking and cytoskeleton remodeling. Exp. Cell Res. 297, 1–10 (2004).
  • Loewen CJ, Gaspar ML, Jesch SA et al.: Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid. Science 304, 1644–1647 (2004).
  • 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).
  • Levine TP, Munro S: Dual targeting of Osh1p, a yeast homologue of oxysterolbinding protein, to both the Golgi and the nucleus-vacuole junction. Mol. Biol. Cell 12, 1633–1644 (2001).
  • Levine T: Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol. 14, 483–490 (2004).
  • Olkkonen VM, Levine TP: Oxysterol binding proteins: in more than one place at one time? Biochem. Cell Biol. 82, 87–98 (2004).
  • 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).
  • 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).
  • 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).
  • 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).
  • 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).
  • Demonstrates that, by using a small interfering RNA-mediated gene-silencing approach, OSBP is not responsible for the effects of 25-hydroxycholesterol on cellular sterol homeostasis.
  • 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).
  • Wyles JP, McMaster CR, Ridgway ND: Vesicle-associated membrane proteinassociated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum. J. Biol. Chem. 277, 29908–29918 (2002).
  • 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).
  • Provides strong evidence for a function of OSBP as a sterol sensor that connects the cellular sterol status with the biosynthesis of sphingomyelin by regulating the function of the ceramide transporter (CERT).
  • 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).
  • Perry RJ, Ridgway ND: Molecular mechanisms and regulation of ceramide transport. Biochim. Biophys. Acta 1734, 220–234 (2005).
  • 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).
  • Reports a new type of signaling function for OSBP: the protein is suggested to act as a sterol-dependent scaffold for two protein phosphatases acting on extracellularregulated kinase (ERK).
  • 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)
  • 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).
  • 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).
  • 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).
  • Reports a new type of connection between ORPs and intracellular membrane trafficking. ORP1L is suggested to act in a complex responsible for the recruitment of dynein/dynactin motors on late endosomes, thus regulating the distribution and function of these compartments.
  • 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).
  • Xu Y, Liu Y, Ridgway ND, McMaster CR: Novel members of the human oxysterolbinding protein family bind phospholipids and regulate vesicle transport. J. Biol. Chem. 276, 18407–18414 (2001).
  • 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).
  • 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).
  • Goldstein JL, DeBose-Boyd RA, Brown MS: Protein sensors for membrane sterols. Cell 124, 35–46 (2006).
  • 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).
  • Tontonoz P, Mangelsdorf DJ: Liver X receptor signaling pathways in cardiovascular disease. Mol. Endocrinol. 17, 985–993 (2003).
  • 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).
  • Beh CT, Cool L, Phillips J, Rine J: Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 157, 1117–1140 (2001).
  • Exhaustive study of S. cerevisiae strains with ORP (OSH) gene disruptions – evidence for a common essential function involving sterol metabolism.
  • Beh CT, Rine J: A role for yeast oxysterolbinding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution. J. Cell Sci. 117, 2983–2996 (2004).
  • Reports that OSH gene disruptions result in a redistribution of cellular ergosterol and, probably as a consequence, in multiple aberrations of cell structure and functions.
  • 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).
  • Provides evidence for a new mechanism regulating the membrane association of ORPs. Yeast Osh6p and Osh7p accumulate on membranes in cells lacking the ATPase Vps4p, associated with a defect in sterol esterification.
  • Fang M, Kearns BG, Gedvilaite A et al.: 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, 6447–6459 (1996).
  • 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).
  • Demonstrates that Osh4p localizes to the yeast Golgi complex, dependent on an interaction with phosphaytidylinositol 4 phosphate and reports evidence for an interplay between Osh4p and the small GTPase ADP-ribosylation factor.
  • Bankaitis VA, Phillips S, Yanagisawa L et al.: Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae. Adv. Enzyme Regul. 45, 155–170 (2005).
  • 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).
  • Provides evidence for a novel type of regulatory function of yeast Osh proteins in cell polarity establishment.
  • Maxfield FR, Wustner D: Intracellular cholesterol transport. J. Clin. Invest. 110, 891–898 (2002).
  • Soccio RE, Breslow JL: Intracellular cholesterol transport. Arterioscler. Thromb. Vasc. Biol. 24, 1150–1160 (2004).
  • Alpy F, Tomasetto C: Give lipids a START: the StAR-related lipid transfer (START) domain in mammals. J. Cell Sci. 118, 2791–2801 (2005).
  • 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).
  • 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).
  • 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).
  • 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).
  • 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).
  • 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).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.