ArticleJournal of lipid research2014
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.
Article in Journal of lipid research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 48 citations in OpenAlex.
- The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.Genetics · 2025Article
- CAP superfamily proteins (VdPRYs) manipulate plant immunity and contribute to the virulence ofMycology · 2025Article
- Membrane Epilipidome-Lipid Modifications, Their Dynamics, and Functional Significance.Cold Spring Harbor perspectives in biology · 2024Review
- Mobilization of cholesterol induces the transition from quiescence to growth in Caenorhabditis elegans through steroid hormone and mTOR signaling.Communications biology · 2024Article
- Ustilago maydis PR-1-like protein has evolved two distinct domains for dual virulence activities.Nature communications · 2023Article
- The function of plant PR1 and other members of the CAP protein superfamily in plant-pathogen interactions.Molecular plant pathology · 2023Review
- Measuring the Interaction of Sterols and Steroids with Proteins by Microscale Thermophoresis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Isolation and Characterization of a Novel Pathogenesis-Related Protein-1 Gene (Plants (Basel, Switzerland) · 2022Article
- Human rs75776403 polymorphism links differential phenotypic and clinical outcomes to a CLEC18A p.T151M-driven multiomics.Journal of biomedical science · 2022Article
- Article
- The yeast cell wall protein Pry3 inhibits mating through highly conserved residues within the CAP domain.Biology open · 2020Article
- Heligmosomoides polygyrus Venom Allergen-like Protein-4 (HpVAL-4) is a sterol binding protein.International journal for parasitology · 2018Article
- Localization and functional characterization of the pathogenesis-related proteins Rbe1p and Rbt4p in Candida albicans.PloS one · 2018Article
- Plant pathogenesis-related proteins of the cacao fungal pathogenThe Journal of biological chemistry · 2017Article
- Tracing the Evolutionary History of the CAP Superfamily of Proteins Using Amino Acid Sequence Homology and Conservation of Splice Sites.Journal of molecular evolution · 2017Article
- Structural insights into the interaction of the conserved mammalian proteins GAPR-1 and Beclin 1, a key autophagy protein.Acta crystallographica. Section D, Structural biology · 2017Article
- Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches' Broom Disease of Cacao.Scientific reports · 2017Article
- The pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is a fatty acid-binding protein.The Journal of biological chemistry · 2017Article
- Structural and functional characterization of the CAP domain of pathogen-related yeast 1 (Pry1) protein.Scientific reports · 2016Article
- DT(270-326) , a Truncated Diphtheria Toxin, Increases Blood-Tumor Barrier Permeability by Upregulating the Expression of Caveolin-1.CNS neuroscience & therapeutics · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 (Pry)1, -2, and -3. We have recently shown that Pry function is required for the secretion of cholesteryl acetate and that Pry proteins bind cholesterol and cholesteryl acetate, suggesting that CAP superfamily members may generally act to bind sterols or related small hydrophobic compounds. Here, we analyzed the mode of sterol binding by Pry1. Computational modeling indicates that ligand binding could occur through displacement of a relatively poorly conserved flexible loop, which in some CAP family members displays homology to the caveolin-binding motif. Point mutations within this motif abrogated export of cholesteryl acetate but did not affect binding of cholesterol. Mutations of residues located outside the caveolin-binding motif, or mutations in highly conserved putative catalytic residues had no effect on export of cholesteryl acetate or on lipid binding. These results indicate that the caveolin-binding motif of Pry1, and possibly of other CAP family members, is crucial for selective lipid binding and that lipid binding may occur through displacement of the loop containing this motif.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.