ArticleThe Journal of biological chemistry2019
Ostreolysin A and anthrolysin O use different mechanisms to control movement of cholesterol from the plasma membrane to the endoplasmic reticulum.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Visualization of the interaction between sphingomyelin and cholesterol in lipid bilayer membranes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Targeting Cellular Lipid Rafts for Dynamic Nuclear Polarization Nuclear Magnetic Resonance.Chembiochem : a European journal of chemical biology · 2026Article
- Review of methods for the determination of cellular cholesterol content: principles, advantages, limitations, applications, and perspectives.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025Review
- Effects of Ethanol and Opioid Receptor Antagonists Naltrexone and LY2444296 on the Organization of Cholesterol- and Sphingomyelin-Enriched Plasma Membrane Domains.ACS chemical neuroscience · 2025Article
- Tetraspanin-enriched membrane domains regulate vascular leakage by altering membrane cholesterol accessibility to balance antagonistic GTPases.Nature cardiovascular research · 2025Article
- Regulation of cellular and systemic sphingolipid homeostasis.Nature reviews. Molecular cell biology · 2024Review
- Visualization of accessible cholesterol using a GRAM domain-based biosensor.Nature communications · 2023Article
- A single point mutation expands the applicability of ostreolysin A6 in biomedicine.Scientific reports · 2023Article
- Cholesterol Transport to the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023Review
- Article
- Sphingosine kinases regulate ER contacts with late endocytic organelles and cholesterol trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cholesterol metabolism: from lipidomics to immunology.Journal of lipid research · 2022Review
- Sphingolipids and Cholesterol.Advances in experimental medicine and biology · 2022Article
- Measuring and Manipulating Membrane Cholesterol for the Study of Hedgehog Signaling.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Host proviral and antiviral factors for SARS-CoV-2.Virus genes · 2021Review
- What Can Mushroom Proteins Teach Us about Lipid Rafts?Membranes · 2021Review
- Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b.The EMBO journal · 2021Article
- The use of anthrolysin O and ostreolysin A to study cholesterol in cell membranes.Methods in enzymology · 2021Article
- Accessibility of cholesterol at cell surfaces.Journal of lipid research · 2020Article
- Last step in the path of LDL cholesterol from lysosome to plasma membrane to ER is governed by phosphatidylserine.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Recent studies using two cholesterol-binding bacterial toxin proteins, perfringolysin O (PFO) and domain 4 of anthrolysin O (ALOD4), have shown that cholesterol in the plasma membranes (PMs) of animal cells resides in three distinct pools. The first pool comprises mobile cholesterol, accessible to both PFO and ALOD4, that is rapidly transported to the endoplasmic reticulum (ER) to signal cholesterol excess and maintain cholesterol homeostasis. The second is a sphingomyelin (SM)-sequestered pool inaccessible to PFO and ALOD4 but that becomes accessible by treatment with SM-degrading sphingomyelinase (SMase). The third is an essential pool also inaccessible to PFO and ALOD4 that cannot be liberated by SMase treatment. The accessible cholesterol pool can be trapped on PMs of live cells by nonlytic ALOD4, blocking its transport to the ER. However, studies of the two other pools have been hampered by a lack of available tools. Here, we used ostreolysin A (OlyA), which specifically binds SM/cholesterol complexes in membranes, to study the SM-sequestered cholesterol pool. Binding of nonlytic OlyA to SM/cholesterol complexes in PMs of live cells depleted the accessible PM cholesterol pool detectable by ALOD4. Consequently, transport of accessible cholesterol from PM to ER ceased, thereby activating SREBP transcription factors and increasing cholesterol synthesis. Thus, OlyA and ALOD4 both control movement of PM cholesterol, but through different lipid-binding mechanisms. We also found that PM-bound OlyA was rapidly internalized into cells, whereas PM-bound ALOD4 remained on the cell surface. Our findings establish OlyA and ALOD4 as complementary tools to investigate cellular cholesterol transport.
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