Evidence map›Paper›PMID 26241960›Full record

ArticlePLoS pathogens2015

Double-Edge Sword of Sustained ROCK Activation in Prion Diseases through Neuritogenesis Defects and Prion Accumulation.

Aurélie Alleaume-Butaux, Simon Nicot, Mathéa Pietri, Anne Baudry, Caroline Dakowski, Philippe Tixador, Hector Ardila-Osorio, Anne-Marie Haeberlé, Yannick Bailly, Jean-Michel Peyrin and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Post-translational modifications in prion diseases.Frontiers in molecular neuroscience · 2024
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Prion Protein: The Molecule of Many Forms and Faces.International journal of molecular sciences · 2022
    Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Retinal Degeneration and Alzheimer's Disease: An Evolving Link.International journal of molecular sciences · 2020
    Review
  14. Prions and prion diseases: Insights from the eye.Experimental eye research · 2020
    Review
  15. Article
  16. Review
  17. RhoA/ROCK Regulates Prion Pathogenesis by Controlling Connexin 43 Activity.International journal of molecular sciences · 2020
    Article
  18. Article
  19. Article
  20. Article
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

13 authors at 7 institutions in 2 countries.

Aurélie Alleaume-ButauxINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Simon NicotINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Mathéa PietriINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Anne BaudryINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Caroline DakowskiINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Philippe TixadorCNRS UMR 8256, Biological Adaptation and Ageing, Paris, France; Sorbonne Université, UPMC Université, Paris 06, UMR 8256, B2A, Biological Adaptation and Ageing, Institut de Biologie Paris Seine, Paris, France.
Hector Ardila-OsorioINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Anne-Marie HaeberléCytologie et Cytopathologie Neuronales, Institut des Neurosciences Cellulaires et Intégratives, CNRS UPR 3212, Strasbourg, France.
Yannick BaillyCytologie et Cytopathologie Neuronales, Institut des Neurosciences Cellulaires et Intégratives, CNRS UPR 3212, Strasbourg, France.
Jean-Michel PeyrinCNRS UMR 8256, Biological Adaptation and Ageing, Paris, France; Sorbonne Université, UPMC Université, Paris 06, UMR 8256, B2A, Biological Adaptation and Ageing, Institut de Biologie Paris Seine, Paris, France.
Jean-Marie LaunayAP-HP, Service de Biochimie, INSERM UMR-S942, Hôpital Lariboisière, Paris, France; Pharma Research Department, Hoffmann La Roche Ltd, Basel, Switzerland.
Odile KellermannINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Benoit SchneiderINSERM, UMR-S 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR-S 1124, Paris, France.
Délégation Paris 5 · FRUniversité Paris Cité · FRCentre National de la Recherche Scientifique · FRInserm · FRAdaptation Biologique et VieillissementSorbonne Paris Cité · FRSorbonne Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In prion diseases, synapse dysfunction, axon retraction and loss of neuronal polarity precede neuronal death. The mechanisms driving such polarization defects, however, remain unclear. Here, we examined the contribution of RhoA-associated coiled-coil containing kinases (ROCK), key players in neuritogenesis, to prion diseases. We found that overactivation of ROCK signaling occurred in neuronal stem cells infected by pathogenic prions (PrPSc) and impaired the sprouting of neurites. In reconstructed networks of mature neurons, PrPSc-induced ROCK overactivation provoked synapse disconnection and dendrite/axon degeneration. This overactivation of ROCK also disturbed overall neurotransmitter-associated functions. Importantly, we demonstrated that beyond its impact on neuronal polarity ROCK overactivity favored the production of PrPSc through a ROCK-dependent control of 3-phosphoinositide-dependent kinase 1 (PDK1) activity. In non-infectious conditions, ROCK and PDK1 associated within a complex and ROCK phosphorylated PDK1, conferring basal activity to PDK1. In prion-infected neurons, exacerbated ROCK activity increased the pool of PDK1 molecules physically interacting with and phosphorylated by ROCK. ROCK-induced PDK1 overstimulation then canceled the neuroprotective α-cleavage of normal cellular prion protein PrPC by TACE α-secretase, which physiologically precludes PrPSc production. In prion-infected cells, inhibition of ROCK rescued neurite sprouting, preserved neuronal architecture, restored neuronal functions and reduced the amount of PrPSc. In mice challenged with prions, inhibition of ROCK also lowered brain PrPSc accumulation, reduced motor impairment and extended survival. We conclude that ROCK overactivation exerts a double detrimental effect in prion diseases by altering neuronal polarity and triggering PrPSc accumulation. Eventually ROCK emerges as therapeutic target to combat prion diseases.

Indexed as

AnimalsBlotting, WesternDisease Models, AnimalFluorescent Antibody TechniqueImmunoprecipitationLab-On-A-Chip DevicesMiceMice, Inbred C57BLNeuritesNeurogenesisPrion DiseasesPrPC ProteinsPrPSc Proteinsrho-Associated KinasesPrPC ProteinsPrPSc Proteinsrho-Associated Kinases

Identifiers

PMID26241960
PMCPMC4524729
OpenAlexW1685885669

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.