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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

ORP2 Delivers Cholesterol to the Plasma Membrane in Exchange for Phosphatidylinositol 4, 5-Bisphosphate (PI(4,5)P2)

Wang, Huan, Ma, Qianli, Qi, Yanfei, Dong, Jiangqing, Du, Ximing, Rae, James, Wang, Jue, Wu, Wei-Feng, Brown, Andrew J., Parton, Robert G., Wu, Jia-Wei, Yang, Hongyuan·2019·Molecular Cell
DOI 10.1016/j.molcel.2018.11.014
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  • Amphotericin B binds PM sterols and eventually causes cell death by various mechanisms, including sequestration of PM sterols and the formation of non-selective ion pores.

    “Amphotericin B binds PM sterols and eventually causes cell death by various mechanisms, including sequestration of PM sterols and the formation of non‐selective ion pores (Kinsky, 1970; Wang et al, 2018).”

    From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Wang et al, 2018

    The Results (page unavailable) report that ORP2-null cells are more resistant to amphotericin B, which the authors interpret as suggesting reduced plasma-membrane cholesterol. The amphotericin B resistance assay (page unavailable) measures surviving cells after exposure. Our copy does not describe sterol sequestration or non-selective ion pores as mechanisms of cell death. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Such enrichment allows for the subsequent transfer of cholesterol to PM by cytoplasmic non-vesicular transfer proteins.

    “and that such enrichment allows for the subsequent transfer of cholesterol to PM by cytoplasmic non-vesicular transfer proteins (42).”

    From Aster-dependent nonvesicular transport facilitates dietary cholesterol uptake (2023) · cites this paper as [42]

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Research works printed but not linked: 41

  1. Adams, 2010, PHENIX: a comprehensive Python-based system for macromolecular structure solution, Acta Crystallogr. D Biol. Crystallogr., 66, 213, 10.1107/S0907444909052925 · DOI · Paper page
  2. Ariotti, 2015, Modular detection of GFP-labeled proteins for rapid screening by electron microscopy in cells and organisms, Dev. Cell, 35, 513, 10.1016/j.devcel.2015.10.016 · DOI
  3. Balla, 2013, Phosphoinositides: tiny lipids with giant impact on cell regulation, Physiol. Rev., 93, 1019, 10.1152/physrev.00028.2012 · DOI · Paper page
  4. Bohdanowicz, 2012, Recruitment of OCRL and Inpp5B to phagosomes by Rab5 and APPL1 depletes phosphoinositides and attenuates Akt signaling, Mol. Biol. Cell, 23, 176, 10.1091/mbc.e11-06-0489 · DOI
  5. Choi, 2016, Agonist-stimulated phosphatidylinositol-3,4,5-trisphosphate generation by scaffolded phosphoinositide kinases, Nat. Cell Biol., 18, 1324, 10.1038/ncb3441 · DOI
  6. Chung, 2015, Intracellular transport. PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts, Science, 349, 428, 10.1126/science.aab1370 · DOI
  7. Das, 2014, Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis, eLife, 3, 10.7554/eLife.02882 · DOI · Paper page
  8. de Saint-Jean, 2011, Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers, J. Cell Biol., 195, 965, 10.1083/jcb.201104062 · DOI
  9. Dong, 2016, Endosome-ER contacts control actin nucleation and retromer function through VAP-dependent regulation of PI4P, Cell, 166, 408, 10.1016/j.cell.2016.06.037 · DOI · Paper page
  10. Du, 2011, A role for oxysterol-binding protein-related protein 5 in endosomal cholesterol trafficking, J. Cell Biol., 192, 121, 10.1083/jcb.201004142 · DOI
  11. Du, 2015, Novel mechanisms of intracellular cholesterol transport: Oxysterol-binding proteins and membrane contact sites, Curr. Opin. Cell Biol., 35, 37, 10.1016/j.ceb.2015.04.002 · DOI
  12. Emsley, 2004, Coot: model-building tools for molecular graphics, Acta Crystallogr. D Biol. Crystallogr., 60, 2126, 10.1107/S0907444904019158 · DOI · Paper page
  13. Ghai, 2017, ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2) and regulate its level at the plasma membrane, Nat. Commun., 8, 757, 10.1038/s41467-017-00861-5 · DOI
  14. Goldstein, 2006, Protein sensors for membrane sterols, Cell, 124, 35, 10.1016/j.cell.2005.12.022 · DOI · Paper page
  15. Hammond, 2012, PI4P and PI(4,5)P2 are essential but independent lipid determinants of membrane identity, Science, 337, 727, 10.1126/science.1222483 · DOI
  16. Humphrey, 1996, VMD: visual molecular dynamics, J. Mol. Graphics, 14, 33, 10.1016/0263-7855(96)00018-5 · DOI · Paper page
  17. Hynynen, 2005, Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis, Biochem. J., 390, 273, 10.1042/BJ20042082 · DOI
  18. Hynynen, 2009, OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids, J. Lipid Res., 50, 1305, 10.1194/jlr.M800661-JLR200 · DOI
  19. Iaea, 2017, Role of STARD4 in sterol transport between the endocytic recycling compartment and the plasma membrane, Mol. Biol. Cell, 28, 1111, 10.1091/mbc.e16-07-0499 · DOI
  20. Ikonen, 2008, Cellular cholesterol trafficking and compartmentalization, Nat. Rev. Mol. Cell Biol., 9, 125, 10.1038/nrm2336 · DOI
  21. Im, 2005, Structural mechanism for sterol sensing and transport by OSBP-related proteins, Nature, 437, 154, 10.1038/nature03923 · DOI
  22. Jansen, 2011, Role of ORPs in sterol transport from plasma membrane to ER and lipid droplets in mammalian cells, Traffic, 12, 218, 10.1111/j.1600-0854.2010.01142.x · DOI
  23. Kentala, 2018, Analysis of ORP2-knockout hepatocytes uncovers a novel function in actin cytoskeletal regulation, FASEB J., 32, 1281, 10.1096/fj.201700604R · DOI
  24. Laitinen, 2002, ORP2, a homolog of oxysterol binding protein, regulates cellular cholesterol metabolism, J. Lipid Res., 43, 245, 10.1016/S0022-2275(20)30166-8 · DOI
  25. Maeda, 2013, Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins, Nature, 501, 257, 10.1038/nature12430 · DOI
  26. Maekawa, 2015, Complementary probes reveal that phosphatidylserine is required for the proper transbilayer distribution of cholesterol, J. Cell Sci., 128, 1422, 10.1242/jcs.164715 · DOI
  27. Maxfield, 2016, Role of STARD4 and NPC1 in intracellular sterol transport, Biochem. Cell Biol., 94, 499, 10.1139/bcb-2015-0154 · DOI
  28. Mesmin, 2016, The counterflow transport of sterols and PI4P, Biochim. Biophys. Acta, 1861, 940, 10.1016/j.bbalip.2016.02.024 · DOI
  29. Mesmin, 2013, A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP, Cell, 155, 830, 10.1016/j.cell.2013.09.056 · DOI
  30. Moser von Filseck, 2015, Intracellular transport. Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate, Science, 349, 432, 10.1126/science.aab1346 · DOI
  31. Olkkonen, 2013, Oxysterol-binding proteins: Sterol and phosphoinositide sensors coordinating transport, signaling and metabolism, Prog. Lipid Res., 52, 529, 10.1016/j.plipres.2013.06.004 · DOI
  32. Otwinowski, 1997, Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol., 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
  33. Perry, 2006, 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, 10.1091/mbc.e06-01-0060 · DOI
  34. Phillips, 2005, Scalable molecular dynamics with NAMD, J. Comput. Chem., 26, 1781, 10.1002/jcc.20289 · DOI · Paper page
  35. Raychaudhuri, 2006, Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides, J. Cell Biol., 173, 107, 10.1083/jcb.200510084 · DOI
  36. Ridgway, 1992, Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding, J. Cell Biol., 116, 307, 10.1083/jcb.116.2.307 · DOI
  37. Schulz, 2009, Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues, J. Cell Biol., 187, 889, 10.1083/jcb.200905007 · DOI
  38. Tong, 2013, Structure of Osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins, Structure, 21, 1203, 10.1016/j.str.2013.05.007 · DOI
  39. Vanommeslaeghe, 2010, CHARMM general force field: a force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields, J. Comput. Chem., 31, 671, 10.1002/jcc.21367 · DOI
  40. Várnai, 1998, Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools, J. Cell Biol., 143, 501, 10.1083/jcb.143.2.501 · DOI · Paper page
  41. Wong, 2017, Advances on the transfer of lipids by lipid transfer proteins, Trends Biochem. Sci., 42, 516, 10.1016/j.tibs.2017.05.001 · DOI

Cited by

Sorted by citations

Metadata

Authors
Wang, H., Ma, Q., Qi, Y., Dong, J., Du, X., Rae, J., Wang, J., Wu, W.-F., Brown, A. J., Parton, R. G., Wu, J.-W., & Yang, H.
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2019-02
Volume
73
Issue
3
Pages
458-473.e7
ISSN
1097-2765
DOI
10.1016/j.molcel.2018.11.014
Cited by
175
References
1
Language
en
Licence
Funders
  • National Health and Medical Research Council (1041301, 1141939, 1144726)
  • NHMRC Senior Research Fellowship (1058237, 2016YFA0502004)
  • National Key R&D Program
  • Ministry of Science and Technology of the People's Republic of China (91754201, 31621063)
  • National Natural Science Foundation of China
  • NHMRC of Australia (APP1037320, APP1058565, APP569542)
  • ARC Center of Excellence in Convergent Bio-Nano Science and Technology

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