Evidence map›Paper›PMID 23530264›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2013

The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability.

Jayne L Elliott, Ming Der Perng, Alan R Prescott, Karin A Jansen, Gijsje H Koenderink, Roy A Quinlan

Open access · bronzeAbstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 54 citations in OpenAlex.

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  9. Review
  10. Desmin variants: Trigger for cardiac arrhythmias?Frontiers in cell and developmental biology · 2022
    Review
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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

6 authors at 3 institutions in 3 countries.

Jayne L ElliottSchool of Biological and Biomedical Sciences, The University of Durham, South Road, Durham DH1 3LE, UK.
Ming Der Perng
Alan R Prescott
Karin A Jansen
Gijsje H Koenderink
Roy A Quinlan
Durham University · GBInstitute for Atomic and Molecular Physics · NLUniversity of Dundee · GB

Funding

PEPFAR 46747
6 · The paper itself

Abstract

CRYAB (αB-crystallin) is expressed in many tissues and yet the R120G mutation in CRYAB causes tissue-specific pathologies, namely cardiomyopathy and cataract. Here, we present evidence to demonstrate that there is a specific functional interaction of CRYAB with desmin intermediate filaments that predisposes myocytes to disease caused by the R120G mutation. We use a variety of biochemical and biophysical techniques to show that plant, animal and ascidian small heat-shock proteins (sHSPs) can interact with intermediate filaments. Nevertheless, the mutation R120G in CRYAB does specifically change that interaction when compared with equivalent substitutions in HSP27 (R140G) and into the Caenorhabditis elegans HSP16.2 (R95G). By transient transfection, we show that R120G CRYAB specifically promotes intermediate filament aggregation in MCF7 cells. The transient transfection of R120G CRYAB alone has no significant effect upon cell viability, although bundling of the endogenous intermediate filament network occurs and the mitochondria are concentrated into the perinuclear region. The combination of R120G CRYAB co-transfected with wild-type desmin, however, causes a significant reduction in cell viability. Therefore, we suggest that while there is an innate ability of sHSPs to interact with and to bind to intermediate filaments, it is the specific combination of desmin and CRYAB that compromises cell viability and this is potentially the key to the muscle pathology caused by the R120G CRYAB.

Indexed as

alpha-Crystallin B ChainAnimalsCell LineCell SurvivalCricetinaeDesminGlial Fibrillary Acidic ProteinHeat-Shock Proteins, SmallHumansHydrogen-Ion ConcentrationMiceMutationProtein BindingProtein ConformationTemperatureVimentinalpha-Crystallin B ChainDesminGlial Fibrillary Acidic ProteinHeat-Shock Proteins, SmallVimentin

Identifiers

PMID23530264
PMCPMC3638400
OpenAlexW2147370131

What OpenQuestion holds

Textmetadata
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.