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

Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae.

Journal of cell science - 1 Oct 2004

Kvam Erik, Goldfarb David S

Abstract excerpt

OSH1 belongs to a seven-member gene family in yeast that is related to mammalian oxysterol-binding protein (OSBP). Here, we investigate the targeting of Osh1p to nucleus-vacuole (NV) junctions in Saccharomyces cerevisiae. NV junctions are interorganelle interfaces mediated by Nvj1p in the nuclear envelope and Vac8p on the vacuole membrane. Together, Nvj1p and Vac8p form Velcro-like patches through which...

Read the complete abstract on PubMed

Topics

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

Share to Aminopeptidases
Share to Autophagy
Share to Golgi Apparatus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipoproteins

Share to Microscopy, Confocal

Share to Microscopy, Immunoelectron

Share to Receptors, Cytoplasmic and Nuclear

Share to Vesicular Transport Proteins

Source

Identifiers

PMID: 15367582
DOI: 10.1242/jcs.01372

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae.PMID 15367582Read ↗

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

A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution.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 ↗

Endosomal Na+ (K+)/H+ exchanger Nhx1/Vps44 functions independently and downstream of multivesicular body formation.Semantic proximity Read ↗

AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism.Semantic proximity Read ↗

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

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

The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae.Semantic proximity Read ↗

The KNH1 gene of Saccharomyces cerevisiae is a functional homolog of KRE9.Semantic proximity Read ↗

Identification and assessment of the role of a nominal phospholipid binding region of ORP1S (oxysterol-binding-protein-related protein 1 short) in the regulation of vesicular transport.Semantic proximity Read ↗

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