ArticleNature communications2019
An electrostatic switching mechanism to control the lipid transfer activity of Osh6p.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Ist2 promotes lipid transfer by Osh6 via its membrane tethering and lipid scramblase activities.Science advances · 2025Article
- Structural basis for lipid transport at membrane contact sites by the IST2-OSH6 complex.Nature structural & molecular biology · 2025Article
- An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025Article
- Coordination of transporter, cargo, and membrane properties during non-vesicular lipid transport.Communications biology · 2024Article
- Unbiased MD simulations identify lipid binding sites in lipid transfer proteins.The Journal of cell biology · 2024Article
- The conformational plasticity of structurally unrelated lipid transport proteins correlates with their mode of action.PLoS biology · 2024Article
- OSBP is a major determinant of Golgi phosphatidylinositol 4-phosphate homeostasis.bioRxiv : the preprint server for biology · 2024Article
- Orthogonal targeting of SAC1 to mitochondria implicates ORP2 as a major player in PM PI4P turnover.bioRxiv : the preprint server for biology · 2024Article
- Reconstitution of ORP-mediated lipid exchange process coupled to PI(4)P metabolism.bioRxiv : the preprint server for biology · 2023Article
- Article
- Ceramide-1-phosphate transfer protein enhances lipid transport by disrupting hydrophobic lipid-membrane contacts.PLoS computational biology · 2023Article
- Up-regulation of Osh6 boosts an anti-aging membrane trafficking pathway toward vacuoles.Microbial cell (Graz, Austria) · 2022Article
- Quantitative Models of Lipid Transfer and Membrane Contact Formation.Contact (Thousand Oaks (Ventura County, Calif.)) · 2022Article
- Functional analyses of phosphatidylserine/PI(4)P exchangers with diverse lipid species and membrane contexts reveal unanticipated rules on lipid transfer.BMC biology · 2021Article
- Ist2 recruits the lipid transporters Osh6/7 to ER-PM contacts to maintain phospholipid metabolism.The Journal of cell biology · 2021Article
- NBD-based synthetic probes for sensing small molecules and proteins: design, sensing mechanisms and biological applications.Chemical Society reviews · 2021Review
- Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels.Frontiers in cell and developmental biology · 2021Review
- Transport Pathways That Contribute to the Cellular Distribution of Phosphatidylserine.Frontiers in cell and developmental biology · 2021Review
- Molecular and cellular dissection of the oxysterol-binding protein cycle through a fluorescent inhibitor.The Journal of biological chemistry · 2020Article
- Lipid Exchangers: Cellular Functions and Mechanistic Links With Phosphoinositide Metabolism.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A central assumption is that lipid transfer proteins (LTPs) bind transiently to organelle membranes to distribute lipids in the eukaryotic cell. Osh6p and Osh7p are yeast LTPs that transfer phosphatidylserine (PS) from the endoplasmic reticulum (ER) to the plasma membrane (PM) via PS/phosphatidylinositol-4-phosphate (PI4P) exchange cycles. It is unknown how, at each cycle, they escape from the electrostatic attraction of the PM, highly anionic, to return to the ER. Using cellular and in vitro approaches, we show that Osh6p reduces its avidity for anionic membranes once it captures PS or PI4P, due to a molecular lid closing its lipid-binding pocket. Thus, Osh6p maintains its transport activity between ER- and PM-like membranes. Further investigations reveal that the lid governs the membrane docking and activity of Osh6p because it is anionic. Our study unveils how an LTP self-limits its residency time on membranes, via an electrostatic switching mechanism, to transfer lipids efficiently.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.