Evidence map›Paper›PMID 27550517›Full record

ArticleJournal of cell science2016

PrP-containing aggresomes are cytosolic components of an ER quality control mechanism.

Tatyana Dubnikov, Tziona Ben-Gedalya, Robert Reiner, Dominic Hoepfner, Wayne A Cabral, Joan C Marini, Ehud Cohen

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020
    Review
  3. Review
  4. Review
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

7 authors at 3 institutions in 3 countries.

Tatyana DubnikovBiochemistry and Molecular Biology, the Institute for Medical Research Israel - Canada (IMRIC), the School of Medicine of the Hebrew University of Jerusalem, Jerusalem 91120, Israel.
Tziona Ben-GedalyaBiochemistry and Molecular Biology, the Institute for Medical Research Israel - Canada (IMRIC), the School of Medicine of the Hebrew University of Jerusalem, Jerusalem 91120, Israel Department of Obstetrics and Gynecology, Hadassah University Hospital, Ein Kerem, Jerusalem, 91120, Israel.
Robert ReinerBiochemistry and Molecular Biology, the Institute for Medical Research Israel - Canada (IMRIC), the School of Medicine of the Hebrew University of Jerusalem, Jerusalem 91120, Israel.
Dominic HoepfnerNovartis Institutes for BioMedical Research, Novartis Campus, Basel 4056, Switzerland.
Wayne A CabralBone and Extracellular Matrix Branch, NICHD, NIH, Bethesda, MD 20892, USA.
Joan C MariniBone and Extracellular Matrix Branch, NICHD, NIH, Bethesda, MD 20892, USA.
Ehud CohenBiochemistry and Molecular Biology, the Institute for Medical Research Israel - Canada (IMRIC), the School of Medicine of the Hebrew University of Jerusalem, Jerusalem 91120, Israel ehudc@ekmd.huji.ac.il.ORCID 0000-0001-5552-7086
Hebrew University of Jerusalem · ILEunice Kennedy Shriver National Institute of Child Health and Human Development · USNovartis (Switzerland) · CH

Funding

Heritable Disorders Of Connective TissueZIAHD000408 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI MARINI, JOAN C · 2009 to 2023
$13.4M
6 · The paper itself

Abstract

Limited detoxification capacity often directs aggregation-prone, potentially hazardous, misfolded proteins to be deposited in designated cytosolic compartments known as 'aggresomes'. The roles of aggresomes as cellular quality control centers, and the cellular origin of the deposits contained within these structures, remain to be characterized. Here, we utilized the observation that the prion protein (PrP, also known as PRNP) accumulates in aggresomes following the inhibition of folding chaperones, members of the cyclophilin family, to address these questions. We found that misfolded PrP molecules must pass through the endoplasmic reticulum (ER) in order to be deposited in aggresomes, that the Golgi plays no role in this process and that cytosolic PrP species are not deposited in pre-existing aggresomes. Prior to their deposition in the aggresome, PrP molecules lose the ER localization signal and have to acquire a GPI anchor. Our discoveries indicate that PrP aggresomes are cytosolic overflow deposition centers for the ER quality control mechanisms and highlight the importance of these structures for the maintenance of protein homeostasis within the ER.

Indexed as

Protein AggregatesAnimalsCHO CellsCricetinaeCricetulusCyclosporineCytosolEndoplasmic ReticulumGlycosylationGlycosylphosphatidylinositolsGolgi ApparatusMice, Inbred C57BLMice, KnockoutModels, BiologicalPrion ProteinsProtein FoldingCyclosporineGlycosylphosphatidylinositolsPrion ProteinsProtein AggregatesAggresomeEndoplasmic reticulumNeurodegenerationPrion proteinProtein aggregation

Identifiers

PMID27550517
PMCPMC6518310
OpenAlexW2511298688

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.