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

The caveolin-binding motif of the pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is required for in vivo export of cholesteryl acetate.

Journal of lipid research - 1 May 2014

Choudhary Vineet, Darwiche Rabih, Gfeller David, Zoete Vincent, Michielin Olivier, Schneiter Roger

Abstract excerpt

Proteins belonging to the CAP superfamily are present in all kingdoms of life and have been implicated in different physiological processes. Their molecular mode of action, however, is poorly understood. Saccharomyces cerevisiae expresses three members of this superfamily, pathogen-related yeast...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Biological Transport
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Caveolins

Share to Cholesterol Esters

Share to Lipid Metabolism

Share to Microfilament Proteins

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 24598142
DOI: 10.1194/jlr.M047126
PMCID: PMC3995466

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-24598142-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The caveolin-binding motif of the pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is required for in vivo export of cholesteryl acetate.PMID 24598142Read ↗

Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.Semantic proximity Read ↗

Structure and function of the ER-Membrane ComplexSemantic proximity Read ↗

The yeast penta-EF protein Pef1p is involved in cation-dependent budding and cell polarization.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 ↗

Association of yeast adenylyl cyclase with cyclase-associated protein CAP forms a second Ras-binding site which mediates its Ras-dependent activation.Semantic proximity Read ↗

A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec1-related Vps33p.Semantic proximity Read ↗

Very long-chain fatty acid-containing lipids rather than sphingolipids per se are required for raft association and stable surface transport of newly synthesized plasma membrane ATPase in yeast.Semantic proximity Read ↗

Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function.Semantic proximity Read ↗

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

The active site of yeast phosphatidylinositol synthase Pis1 is facing the cytosol.Semantic proximity Read ↗

Direct link between RACK1 function and localization at the ribosome in vivo.Semantic proximity Read ↗

ABC Transporters in Saccharomyces cerevisiae and Their Interactors: New Technology Advances the Biology of the ABCC (MRP) SubfamilySemantic proximity Read ↗

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