ArticleMolecular biology of the cell2013
Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Dynamic assessment of PI4P metabolism using split GFP based sensors.Scientific reports · 2025Article
- Inhibition of OSBP blocks retrograde trafficking by inducing partial Golgi degradation.Nature chemical biology · 2025Article
- HCMV strain- and cell type-specific alterations in membrane contact sites point to the convergent regulation of organelle remodeling.Journal of virology · 2024Article
- Single-molecule localization microscopy reveals STING clustering at the trans-Golgi network through palmitoylation-dependent accumulation of cholesterol.Nature communications · 2024Article
- Golgi-Targeting Anticancer Natural Products.Cancers · 2023Review
- Review
- A cell-free assay implicates a role of sphingomyelin and cholesterol in STING phosphorylation.Scientific reports · 2021Article
- The ER cholesterol sensor SCAP promotes CARTS biogenesis at ER-Golgi membrane contact sites.The Journal of cell biology · 2021Article
- Bridging the molecular and biological functions of the oxysterol-binding protein family.Cellular and molecular life sciences : CMLS · 2018Review
- Control of insulin granule formation and function by the ABC transporters ABCG1 and ABCA1 and by oxysterol binding protein OSBP.Molecular biology of the cell · 2018Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) have been implicated in the distribution of sterols among intracellular organelles. OSBP regulates the Golgi cholesterol level, but how it relates to Golgi function is elusive. Here we report that OSBP is essential for the localization of intra-Golgi soluble vesicle N-ethylmaleimide-sensitive fusion attachment protein receptors (v-SNAREs). Depletion of OSBP by small interfering RNA causes mislocalization of intra-Golgi v-SNAREs GS28 and GS15 throughout the cytoplasm without affecting the perinuclear localization of Golgi target-SNARE syntaxin5 and reduces the abundance of a Golgi enzyme, mannosidase II (Man II). GS28 mislocalization and Man II reduction are also induced by cellular cholesterol depletion. Three domains of OSBP-an endoplasmic reticulum-targeting domain, a Golgi-targeting domain, and a sterol-binding domain-are all required for Golgi localization of GS28. Finally, GS28 mislocalization and Man II reduction in OSBP-depleted cells are largely restored by depletion of ArfGAP1, a regulator of the budding of coat protein complex (COP)-I vesicles. From these results, we postulate that Golgi cholesterol level, which is controlled by OSBP, is essential for Golgi localization of intra-Golgi v-SNAREs by ensuring proper COP-I vesicle transport.
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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.