CoChat
Sign Up
Cited by 39

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

Ostreolysin A and anthrolysin O use different mechanisms to control movement of cholesterol from the plasma membrane to the endoplasmic reticulum

Johnson, Kristen A., Endapally, Shreya, Vazquez, Danya C., Infante, Rodney E., Radhakrishnan, Arun·2019·Journal of Biological Chemistry
DOI 10.1074/jbc.ra119.010393
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.ra119.010393

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Artificially trapping accessible cholesterol in the plasma membrane results in constitutive activation of SREBPs and dysregulated cholesterol metabolism.

    “Artificially trapping accessible cholesterol in the PM results in constitutive activation of SREBPs and dysregulated cholesterol metabolism (Infante & Radhakrishnan, 2017; Johnson et al, 2019).”

    From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Johnson et al, 2019

    The Abstract reports that trapping accessible PM cholesterol with ALOD4 activates SREBP despite cholesterol being above its normal threshold. The section “Binding of OlyA lowers ER cholesterol levels” also reports increased HMGCR, supporting disrupted cholesterol regulation. “Constitutive” overstates the finding: that section shows 25-hydroxycholesterol could still suppress SREBP2 activation during ALOD4 treatment. No page numbers are available in our copy. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • Other widely used toxin-based biosensors for accessible cholesterol, including D4 of ALO and PFO, are useful for measuring levels of accessible cholesterol in the PM, but they trap accessible cholesterol in the PM and induce dysregulation of cholesterol homeostasis.

    “Other widely used toxin‐based biosensors for accessible cholesterol, including D4 of ALO and PFO, are useful for measuring levels of accessible cholesterol in the PM, but they trap accessible cholesterol in the PM and induce dysregulation of cholesterol homeostasis (Infante & Radhakrishnan, 2017; Johnson et al, 2019).”

    From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Johnson et al, 2019

    Split into 2 atoms — 1 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.

    Experimental — accuracy not yet measured

  • The accessible pool of cholesterol is the only pool that is free to move to the ER to exert regulatory actions.

    “The accessible pool of cholesterol is the only pool that is free to move to the ER to exert regulatory actions (7, 8, 29).”

    From Last step in the path of LDL cholesterol from lysosome to plasma membrane to ER is governed by phosphatidylserine (2020) · cites this paper as [29]

  • Treatment with sphingomyelinase releases cholesterol from sphingomyelin, thereby increasing the accessible pool.

    “Treatment with sphingomyelinase releases cholesterol from sphingomyelin, thereby increasing the accessible pool.”

    From Last step in the path of LDL cholesterol from lysosome to plasma membrane to ER is governed by phosphatidylserine (2020) · cites this paper as [29]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 41

  1. Brown, 2018, Retrospective on cholesterol homeostasis: the central role of scap, Annu. Rev. Biochem, 87, 783, 10.1146/annurev-biochem-062917-011852 · DOI · Paper page
  2. Horton, 2002, SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver, J. Clin. Invest, 109, 1125, 10.1172/JCI0215593 · DOI · Paper page
  3. Wattenberg, 1983, Sterol partitioning among intracellular membranes, J. Biol. Chem, 258, 2284, 10.1016/S0021-9258(18)32920-X · DOI
  4. Xu, 1991, Lipoproteins activate acyl-coenzyme A:cholesterol acyltransferase in macrophages only after cellular cholesterol pools are expanded to a critical threshold level, J. Biol. Chem, 266, 17040, 10.1016/S0021-9258(19)47337-7 · DOI
  5. Neufeld, 1996, Intracellular trafficking of cholesterol monitored with a cyclodextrin, J. Biol. Chem, 271, 21604, 10.1074/jbc.271.35.21604 · DOI
  6. Underwood, 1998, Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane, J. Biol. Chem, 273, 4266, 10.1074/jbc.273.7.4266 · DOI
  7. Lange, 2004, How cholesterol homeostasis is regulated by plasma membrane cholesterol in excess of phospholipids, Proc. Natl. Acad. Sci. U.S.A, 101, 11664, 10.1073/pnas.0404766101 · DOI
  8. Luo, 2019, Intracellular cholesterol transport by sterol transfer proteins at membrane contact sites, Trends Biochem. Sci, 44, 273, 10.1016/j.tibs.2018.10.001 · DOI
  9. Das, 2014, Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis, Elife, 3, e02882, 10.7554/eLife.02882 · DOI · Paper page
  10. Infante, 2017, Continuous transport of a small fraction of plasma membrane cholesterol to endoplasmic reticulum regulates total cellular cholesterol, Elife, 6, e25466, 10.7554/eLife.25466 · DOI · Paper page
  11. Das, 2013, Use of mutant 125I-perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells, Proc. Natl. Acad. Sci. U.S.A, 110, 10580, 10.1073/pnas.1309273110 · DOI · Paper page
  12. Sokolov, 2010, Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold, J. Biol. Chem, 285, 29480, 10.1074/jbc.M110.148254 · DOI · Paper page
  13. Flanagan, 2009, Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding, Biochemistry, 48, 3977, 10.1021/bi9002309 · DOI
  14. Scheek, 1997, Sphingomyelin depletion in cultured cells blocks proteolysis of sterol regulatory element binding proteins at site 1, Proc. Natl. Acad. Sci. U.S.A, 94, 11179, 10.1073/pnas.94.21.11179 · DOI · Paper page
  15. Slotte, 1988, Depletion of plasma membrane sphingomyelin rapidly alters the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts, Biochem. J, 250, 653, 10.1042/bj2500653 · DOI · Paper page
  16. Endapally, 2019, Molecular discrimination between two conformations of sphingomyelin in plasma membranes, Cell, 176, 1040, 10.1016/j.cell.2018.12.042 · DOI · Paper page
  17. Simons, 2000, How cells handle cholesterol, Science, 290, 1721, 10.1126/science.290.5497.1721 · DOI
  18. McConnell, 2003, Condensed complexes of cholesterol and phospholipids, Biochim. Biophys. Acta, 1610, 159, 10.1016/S0005-2736(03)00015-4 · DOI · Paper page
  19. Skočaj, 2014, Tracking cholesterol/sphingomyelin-rich membrane domains with the ostreolysin A-mCherry protein, PLoS ONE, 9, e92783, 10.1371/journal.pone.0092783 · DOI
  20. Bourdeau, 2009, Cellular functions and X-ray structure of anthrolysin O, a cholesterol-dependent cytolysin secreted by Bacillus anthracis, J. Biol. Chem, 284, 14645, 10.1074/jbc.M807631200 · DOI
  21. Lukoyanova, 2015, Conformational changes during pore formation by the perforin-related protein pleurotolysin, PLoS Biol, 13, e1002049, 10.1371/journal.pbio.1002049 · DOI
  22. Brown, 1990, Regulation of the mevalonate pathway, Nature, 43, 425
  23. Goldstein, 1983, Receptor-mediated endocytosis of low-density lipoprotein in cultured cells, Methods Enzymol, 98, 241, 10.1016/0076-6879(83)98152-1 · DOI
  24. Chang, 2006, Cholesterol sensing, trafficking, and esterification, Annu. Rev. Cell Dev. Biol, 22, 129, 10.1146/annurev.cellbio.22.010305.104656 · DOI
  25. Kovanen, 1981, Saturation and suppression of hepatic lipoprotein receptors: a mechanism for the hypercholesterolemia of cholesterol-fed rabbits, Proc. Natl. Acad. Sci. U.S.A, 78, 1396, 10.1073/pnas.78.3.1396 · DOI
  26. Adams, 2004, Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and insigs, J. Biol. Chem, 279, 52772, 10.1074/jbc.M410302200 · DOI
  27. Radhakrishnan, 2007, Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig, Proc. Natl. Acad. Sci. U.S.A, 104, 6511, 10.1073/pnas.0700899104 · DOI · Paper page
  28. Wojtanik, 2003, The transport of low density lipoprotein-derived cholesterol to the plasma membrane is defective in NPC1 cells, J. Biol. Chem, 278, 14850, 10.1074/jbc.M300488200 · DOI
  29. Liscum, 1987, Low density lipoprotein (LDL)-mediated suppression of cholesterol synthesis and LDL uptake is defective in Niemann-Pick type C fibroblasts, J. Biol. Chem, 262, 17002, 10.1016/S0021-9258(18)45483-X · DOI
  30. Pentchev, 2004, Niemann-Pick C research from mouse to gene, Biochim. Biophys. Acta, 1685, 3, 10.1016/j.bbalip.2004.08.005 · DOI
  31. Kwon, 2009, Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol, Cell, 137, 1213, 10.1016/j.cell.2009.03.049 · DOI · Paper page
  32. Chakrabarti, 2017, Variability of cholesterol accessibility in human red blood cells measured using a bacterial cholesterol-binding toxin, Elife, 6, e23355, 10.7554/eLife.23355 · DOI
  33. Lakshminarayan, 2014, Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers, Nat. Cell Biol, 16, 595, 10.1038/ncb2970 · DOI
  34. Keller, 2000, Saturated phospholipids with high melting temperatures form complexes with cholesterol in monolayers, J. Phys. Chem. B, 104, 7522, 10.1021/jp000958g · DOI
  35. Lange, 2013, Stability and stoichiometry of bilayer phospholipid-cholesterol complexes: relationship to cellular sterol distribution and homeostasis, Biochemistry, 52, 6950, 10.1021/bi400862q · DOI · Paper page
  36. Liscum, 1983, Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase and its mRNA in rat liver as studied with a monoclonal antibody and a cDNA probe, J. Biol. Chem, 258, 8450, 10.1016/S0021-9258(20)82085-7 · DOI
  37. Gay, 2015, Switch-like responses of two cholesterol sensors do not require protein oligomerization in membranes, Biophys. J, 108, 1459, 10.1016/j.bpj.2015.02.008 · DOI · Paper page
  38. Endapally, 2019, Monitoring and modulating intracellular cholesterol trafficking using ALOD4, a cholesterol-binding protein, Methods Mol. Biol, 1949, 153, 10.1007/978-1-4939-9136-5_12 · DOI
  39. McDonald, 2012, A comprehensive method for extraction and quantitative analysis of sterols and secosteroids from human plasma, J. Lipid Res, 53, 1399, 10.1194/jlr.D022285 · DOI
  40. Apostolopoulou, 2018, Specific hepatic sphingolipids relate to insulin resistance, oxidative stress, and inflammation in nonalcoholic steatohepatitis, Diabetes Care, 41, 1235, 10.2337/dc17-1318 · DOI · Paper page
  41. Goldstein, 1974, Binding and degradation of low density lipoproteins by cultured human fibroblasts. Comparison of cells from a normal subject and from a patient with homozygous familial hypercholesterolemia, J. Biol. Chem, 249, 5153, 10.1016/S0021-9258(19)42341-7 · DOI · Paper page

Cited by

Sorted by citations

Metadata

Authors
Johnson, K. A., Endapally, S., Vazquez, D. C., Infante, R. E., & Radhakrishnan, A.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2019-11
Volume
294
Issue
46
Pages
17289-17300
ISSN
0021-9258
DOI
10.1074/jbc.ra119.010393
Cited by
39
References
1
Language
en
Licence
Funders
  • HHS | National Institutes of Health (HL20948)
  • Welch Foundation (I-1793)
  • Burroughs Wellcome Fund (1019692)
  • American Gastroenterological Association (2019AGARSA3)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review