ArticlePloS one2014
Characterization of the sterol and phosphatidylinositol 4-phosphate binding properties of Golgi-associated OSBP-related protein 9 (ORP9).
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Key Mechanisms in Lysosome Stability, Degradation and Repair.Molecular and cellular biology · 2025Review
- Regulation of cellular cholesterol distribution via non-vesicular lipid transport at ER-Golgi contact sites.Nature communications · 2023Article
- ORP9 and ORP10 form a heterocomplex to transfer phosphatidylinositol 4-phosphate at ER-TGN contact sites.Cellular and molecular life sciences : CMLS · 2023Article
- Review
- Roles of Phosphatidylinositol 4-Phosphorylation in Non-vesicular Cholesterol Trafficking.Advances in experimental medicine and biology · 2023Article
- Article
- PI4P/PS countertransport by ORP10 at ER-endosome membrane contact sites regulates endosome fission.The Journal of cell biology · 2022Article
- Functions of Oxysterol-Binding Proteins at Membrane Contact Sites and Their Control by Phosphoinositide Metabolism.Frontiers in cell and developmental biology · 2021Review
- YPIBP: A repository for phosphoinositide-binding proteins in yeast.Computational and structural biotechnology journal · 2021Article
- Cellular homeostasis in theMolecular biology of the cell · 2020Article
- Lipid Exchangers: Cellular Functions and Mechanistic Links With Phosphoinositide Metabolism.Frontiers in cell and developmental biology · 2020Review
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- Bridging the molecular and biological functions of the oxysterol-binding protein family.Cellular and molecular life sciences : CMLS · 2018Review
- The Rab11-binding protein RELCH/KIAA1468 controls intracellular cholesterol distribution.The Journal of cell biology · 2018Article
- Oxysterol-binding Protein Activation at Endoplasmic Reticulum-Golgi Contact Sites Reorganizes Phosphatidylinositol 4-Phosphate Pools.The Journal of biological chemistry · 2016Article
- Ligand-dependent localization and function of ORP-VAP complexes at membrane contact sites.Cellular and molecular life sciences : CMLS · 2015Article
- OSBP-Related Protein Family in Lipid Transport Over Membrane Contact Sites.Lipid insights · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Oxysterol binding protein (OSBP) and OSBP-related proteins (ORPS) have a conserved lipid-binding fold that accommodates cholesterol, oxysterols and/or phospholipids. The diversity of OSBP/ORPs and their potential ligands has complicated the analysis of transfer and signalling properties of this mammalian gene family. In this study we explored the use of the fluorescent sterol cholestatrienol (CTL) to measure sterol binding by ORP9 and competition by other putative ligands. Relative to cholesterol, CTL and dehydroergosterol (DHE) were poor ligands for OSBP. In contrast, both long (ORP9L) and short (ORP9S) variants of ORP9 rapidly extracted CTL, and to a lesser extent DHE, from liposomes. ORP9L and ORP9S also extracted [32P]phosphatidylinositol 4-phosphate (PI-4P) from liposomes, which was inhibited by mutating two conserved histidine residues (HH488,489AA) at the entrance to the binding pocket but not by a mutation in the lid region that inhibited cholesterol binding. Results of direct binding and competition assays showed that phosphatidylserine was poorly extracted from liposomes by ORP9 compared to CTL and PI-4P. ORP9L and PI-4P did not co-localize in the trans-Golgi/TGN of HeLa cells, and siRNA silencing of ORP9L expression did not affect PI-4P distribution in the Golgi apparatus. However, transient overexpression of ORP9L or ORP9S in CHO cells, but not the corresponding PI-4P binding mutants, prevented immunostaining of Golgi-associated PI-4P. The apparent sequestration of Golgi PI-4P by ORP9S was identified as a possible mechanism for its growth inhibitory effects. These studies identify ORP9 as a dual sterol/PI-4P binding protein that could regulate PI-4P in the Golgi apparatus.
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Registered trials
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.