Evidence map›Paper›PMID 22453173›Full record

ArticlePrion

Two-steps control of cellular prion physiology by the extracellular regulated kinase-1 (ERK1).

Frédéric Checler

Abstract read
In one paragraph

Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Proteolytic processing of the prion protein in health and disease.American journal of neurodegenerative disease · 2012
    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

1 author.

Frédéric CheclerInstitut de Pharmacologie Moléculaire et Cellulaire and Institut de NeuroMédecine Moléculaire, Equipe labellisée Fondation pour la Recherche Médicale, Valbonne, France. checler@ipmc.cnrs.fr

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular prion (PrP(c)) undergoes a regulated α-secretase-like cleavage by the disintegrin ADAM17 similar to the one taking place on β-amyloid precursor protein (βAPP). Because these cleavages give rise to biologically active fragments, understanding their regulation could be of importance. We have established that the Extracellular Regulated Kinase-1 (ERK1) controls PrPc processing by modulating ADAM17 phosphorylation in a protein kinase C-dependent manner. Strikingly, we also demonstrated that ERK1 acts upstream to increase PrP(c) promoter transactivation in an AP-1 dependent manner. Therefore, ERK1 exerts a dual control of both PrP(c) metabolism and expression. Interestingly, α-secretase cleavage of βAPP appears to be independent of ERK1. I describe here similarities and differences in α-secretase-mediated PrP(c) and βAPP processing pathways and discuss putative physiopathological implications.

Indexed as

ADAM17 ProteinADAM ProteinsAmyloid beta-Protein PrecursorAnimalsHumansMitogen-Activated Protein Kinase 3Models, BiologicalPrionsProtein Processing, Post-TranslationalADAM17 ProteinADAM17 protein, humanADAM ProteinsAmyloid beta-Protein PrecursorMitogen-Activated Protein Kinase 3Prions

Identifiers

PMID22453173
PMCPMC3338960

What OpenQuestion holds

Textmetadata
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.