Evidence map›Paper›PMID 28238655›Full record

ArticleCurrent biology : CB2017

RTN3 Is a Novel Cold-Induced Protein and Mediates Neuroprotective Effects of RBM3.

Amandine Bastide, Diego Peretti, John R P Knight, Stefano Grosso, Ruth V Spriggs, Xavier Pichon, Thomas Sbarrato, Anne Roobol, Jo Roobol, Davide Vito and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 84 citations in OpenAlex.

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  12. SMYD5 is a regulator of the mild hypothermia response.bioRxiv : the preprint server for biology · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 2 institutions in 1 country.

Amandine BastideMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK.
Diego PerettiMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK; Department of Clinical Neurosciences, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0AH, UK.
John R P KnightMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK.
Stefano GrossoMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK.
Ruth V SpriggsMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK.
Xavier PichonMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK.
Thomas SbarratoMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK.
Anne RoobolCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Jo RoobolCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Davide VitoCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Martin BushellMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK.
Tobias von der HaarCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
C Mark SmalesCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK. Electronic address: c.m.smales@kent.ac.uk.
Giovanna R MallucciMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK; Department of Clinical Neurosciences, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0AH, UK. Electronic address: gm522@cam.ac.uk.
Anne E WillisMedical Research Council Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK. Electronic address: aew5@le.ac.uk.
Medical Research Council · GBUniversity of Kent · GB

Funding

Medical Research Council MC_EX_G0902052Medical Research Council MC_U123160654Medical Research Council MC_U132692719Medical Research Council MC_UP_A600_1023Medical Research Council MC_UP_A600_1024Medical Research Council MR/M501773/1
6 · The paper itself

Abstract

Cooling and hypothermia are profoundly neuroprotective, mediated, at least in part, by the cold shock protein, RBM3. However, the neuroprotective effector proteins induced by RBM3 and the mechanisms by which mRNAs encoding cold shock proteins escape cooling-induced translational repression are unknown. Here, we show that cooling induces reprogramming of the translatome, including the upregulation of a new cold shock protein, RTN3, a reticulon protein implicated in synapse formation. We report that this has two mechanistic components. Thus, RTN3 both evades cooling-induced translational elongation repression and is also bound by RBM3, which drives the increased expression of RTN3. In mice, knockdown of RTN3 expression eliminated cooling-induced neuroprotection. However, lentivirally mediated RTN3 overexpression prevented synaptic loss and cognitive deficits in a mouse model of neurodegeneration, downstream and independently of RBM3. We conclude that RTN3 expression is a mediator of RBM3-induced neuroprotection, controlled by novel mechanisms of escape from translational inhibition on cooling.

Indexed as

AnimalsCold Shock Proteins and PeptidesCold-Shock ResponseCold TemperatureHEK293 CellsHumansMiceNerve Tissue ProteinsNeuroprotective AgentsRNA-Binding ProteinsCold Shock Proteins and PeptidesNerve Tissue ProteinsNeuroprotective AgentsRbm3 protein, mouseRNA-Binding ProteinsRtn3 protein, mousecold shockmRNA translationneuroprotectionprotein synthesisRBM3RTN3

Identifiers

PMID28238655
PMCPMC5344685
OpenAlexW2590271726

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.