Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Multisite phosphorylation of oxysterol-binding protein regulates sterol binding and activation of sphingomyelin synthesis.

Molecular biology of the cell - 1 Sept 2012

Goto Asako, Liu Xinwei, Robinson Carolyn-Ann, Ridgway Neale D

Abstract excerpt

The endoplasmic reticulum (ER)-Golgi sterol transfer activity of oxysterol-binding protein (OSBP) regulates sphingomyelin (SM) synthesis, as well as post-Golgi cholesterol efflux pathways. The phosphorylation and ER-Golgi localization of OSBP are correlated, suggesting this modification regulates the directionality and/or specificity of transfer activity. In this paper, we report that phosphorylation on two...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding, Competitive
Share to Golgi Apparatus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydroxycholesterols

Share to Microscopy, Electron, Transmission

Share to Receptors, Steroid

Share to Sf9 Cells

Share to Sphingomyelins

Share to Sterols

Source

Open in PubMed Open full text

Identifiers

PMID: 22875984
DOI: 10.1091/mbc.E12-04-0283
PMCID: PMC3442410

Genes

OSBP

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multisite phosphorylation of oxysterol-binding protein regulates sterol binding and activation of sphingomyelin synthesis.PMID 22875984Read ↗

Oxysterol-binding Protein Activation at Endoplasmic Reticulum-Golgi Contact Sites Reorganizes Phosphatidylinositol 4-Phosphate Pools.Semantic proximity Read ↗

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

Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum.Semantic proximity Read ↗

Characterization of the sterol and phosphatidylinositol 4-phosphate binding properties of Golgi-associated OSBP-related protein 9 (ORP9).Semantic proximity Read ↗

Orm proteins integrate multiple signals to maintain sphingolipid homeostasis.Semantic proximity Read ↗

Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues.Semantic proximity Read ↗

Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides.Semantic proximity Read ↗

Reversible phosphorylation as a molecular switch to regulate plasma membrane targeting of acylated SH4 domain proteins.Semantic proximity Read ↗

Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), AND SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase.Semantic proximity Read ↗

Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs.Semantic proximity Read ↗

Phosphoregulation of the ceramide transport protein CERT at serine 315 in the interaction with VAMP-associated protein (VAP) for inter-organelle trafficking of ceramide in mammalian cells.Semantic proximity Read ↗

VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.