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Article

Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction.

Molecular biology of the cell - 1 Jun 2001

Levine T P, Munro S

Abstract excerpt

Oxysterol binding protein (OSBP) is the only protein known to bind specifically to the group of oxysterols with potent effects on cholesterol homeostasis. Although the function of OSBP is currently unknown, an important role is implicated by the existence of multiple homologues in all eukaryotes so far examined. OSBP and a subset of homologues contain pleckstrin homology (PH) domains. Such domains are responsible...

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Identifiers

PMID: 11408574
DOI: 10.1091/mbc.12.6.1633
PMCID: PMC37330

Genes

OSBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction.PMID 11408574Read ↗

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Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae.Semantic proximity Read ↗

The sterol-binding protein Kes1/Osh4p is a regulator of polarized exocytosis.Semantic proximity Read ↗

Overlapping functions of the yeast oxysterol-binding protein homologues.Semantic proximity Read ↗

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Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis.Semantic proximity Read ↗

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