Evidence map›Paper›PMID 19503793›Full record

ArticlePloS one2009

Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells.

Daniela Sarnataro, Anna Caputo, Philippe Casanova, Claudia Puri, Simona Paladino, Simona S Tivodar, Vincenza Campana, Carlo Tacchetti, Chiara Zurzolo

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Membrane Rafts: Portals for Viral Entry.Frontiers in microbiology · 2021
    Review
  8. Time-Dependent Internalization of S100B by Mesenchymal Stem CellsFrontiers in cell and developmental biology · 2021
    Article
  9. A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020
    Review
  10. Review
  11. Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019
    Review
  12. Microbiome Influence in the Pathogenesis of Prion and Alzheimer's Diseases.International journal of molecular sciences · 2019
    Review
  13. Review
  14. Article
  15. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Daniela SarnataroDipartimento di Biologia e Patologia Cellulare e Molecolare, Università degli Studi di Napoli Federico II, Napoli, Italy.
Anna Caputo
Philippe Casanova
Claudia Puri
Simona Paladino
Simona S Tivodar
Vincenza Campana
Carlo Tacchetti
Chiara Zurzolo
University of Naples Federico II · ITInstitut Pasteur · FRFIRC Institute of Molecular Oncology · ITUniversity of Genoa · IT

Funding

Telethon GGP04147
6 · The paper itself

Abstract

backgroundThe cellular prion protein (PrP(C)) plays a key role in the pathogenesis of Transmissible Spongiform Encephalopathies in which the protein undergoes post-translational conversion to the infectious form (PrP(Sc)). Although endocytosis appears to be required for this conversion, the mechanism of PrP(C) internalization is still debated, as caveolae/raft- and clathrin-dependent processes have all been reported to be involved. METHODOLOGY/PRINCIPAL

findingsWe have investigated the mechanism of PrP(C) endocytosis in Fischer Rat Thyroid (FRT) cells, which lack caveolin-1 (cav-1) and caveolae, and in FRT/cav-1 cells which form functional caveolae. We show that PrP(C) internalization requires activated Cdc-42 and is sensitive to cholesterol depletion but not to cav-1 expression suggesting a role for rafts but not for caveolae in PrP(C) endocytosis. PrP(C) internalization is also affected by knock down of clathrin and by the expression of dominant negative Eps15 and Dynamin 2 mutants, indicating the involvement of a clathrin-dependent pathway. Notably, PrP(C) co-immunoprecipitates with clathrin and remains associated with detergent-insoluble microdomains during internalization thus indicating that PrP(C) can enter the cell via multiple pathways and that rafts and clathrin cooperate in its internalization. CONCLUSIONS/SIGNIFICANCE: These findings are of particular interest if we consider that the internalization route/s undertaken by PrP(C) can be crucial for the ability of different prion strains to infect and to replicate in different cell lines.

Indexed as

AnimalsCalcium-Binding ProteinsCaveolaeCaveolin 1cdc42 GTP-Binding ProteinCholesterolClathrinDynamin IIEndocytosisGenes, DominantIntracellular Signaling Peptides and ProteinsMembrane MicrodomainsPrionsRatsRats, Inbred F344Thyroid GlandCalcium-Binding ProteinsCaveolin 1cdc42 GTP-Binding ProteinCholesterolClathrinDynamin IIEps15 protein, ratIntracellular Signaling Peptides and ProteinsPrions

Identifiers

PMID19503793
PMCPMC2688078
OpenAlexW2071609717

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.