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Article

Oxysterol-binding protein recruitment and activity at the endoplasmic reticulum-Golgi interface are independent of Sac1.

Traffic (Copenhagen, Denmark) - 1 Aug 2017

Charman Mark, Goto Asako, Ridgway Neale D

Abstract excerpt

Oxysterol-binding protein (OSBP) localizes to endoplasmic reticulum (ER)-Golgi contact sites where it transports cholesterol and phosphatidylinositol 4-phosphate (PI-4P), and activates lipid transport and biosynthetic activities. The PI-4P phosphatase Sac1 cycles between the ER and Golgi apparatus where it potentially regulates OSBP activity. Here we examined whether the ER-Golgi distribution of endogenous or...

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Source

Identifiers

PMID: 28471037
DOI: 10.1111/tra.12491

Genes

OSBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Oxysterol-binding protein recruitment and activity at the endoplasmic reticulum-Golgi interface are independent of Sac1.PMID 28471037Read ↗

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Multisite phosphorylation of oxysterol-binding protein regulates sterol binding and activation of sphingomyelin synthesis.Semantic proximity Read ↗

Regulation of intracellular phosphatidylinositol-4-phosphate by the Sac1 lipid phosphatase.Semantic proximity Read ↗

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