Evidence map›Paper›PMID 33314263›Full record

ArticlePlant, cell & environment2021

Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance.

Anthony Guihur, Bruno Fauvet, Andrija Finka, Manfredo Quadroni, Pierre Goloubinoff

Open access · bronzeAbstract read
In one paragraph

Article in Plant, cell & environment, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. BPM Proteins Modulate Heat Stress Response inPlants (Basel, Switzerland) · 2025
    Article
  6. Review
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  14. RNA Sequencing ofInternational journal of molecular sciences · 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

5 authors at 2 institutions in 2 countries.

Anthony GuihurDepartment of Plant Molecular Biology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0001-5353-1428
Bruno FauvetDepartment of Plant Molecular Biology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0001-5775-3001
Andrija FinkaDepartment of Ecology, Agronomy and Aquaculture, University of Zadar, Zadar, Croatia.ORCID 0000-0001-7608-4771
Manfredo QuadroniProtein Analysis Facility, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0002-2720-4084
Pierre GoloubinoffDepartment of Plant Molecular Biology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0002-4802-0807
University of Lausanne · CHUniversity of Zadar · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

At dawn of a scorching summer day, land plants must anticipate upcoming extreme midday temperatures by timely establishing molecular defences that can keep heat-labile membranes and proteins functional. A gradual morning pre-exposure to increasing sub-damaging temperatures induces heat-shock proteins (HSPs) that are central to the onset of plant acquired thermotolerance (AT). To gain knowledge on the mechanisms of AT in the model land plant Physcomitrium patens, we used label-free LC-MS/MS proteomics to quantify the accumulated and depleted proteins before and following a mild heat-priming treatment. High protein crowding is thought to promote protein aggregation, whereas molecular chaperones prevent and actively revert aggregation. Yet, we found that heat priming (HP) did not accumulate HSP chaperones in chloroplasts, although protein crowding was six times higher than in the cytosol. In contrast, several HSP20s strongly accumulated in the cytosol, yet contributing merely 4% of the net mass increase of heat-accumulated proteins. This is in poor concordance with their presumed role at preventing the aggregation of heat-labile proteins. The data suggests that under mild HP unlikely to affect protein stability. Accumulating HSP20s leading to AT, regulate the activity of rare and specific signalling proteins, thereby preventing cell death under noxious heat stress.

Indexed as

BryopsidaChromatography, LiquidCytosolGene Expression Regulation, PlantHeat-Shock ProteinsHSP20 Heat-Shock ProteinsMolecular ChaperonesMultiprotein ComplexesPhotosystem II Protein ComplexPlant ProteinsProteomicsTandem Mass SpectrometryThermotoleranceWorkflowHeat-Shock ProteinsHSP20 Heat-Shock ProteinsMolecular ChaperonesMultiprotein ComplexesPhotosystem II Protein ComplexPlant Proteinsheat-primingheat-shock proteinsheat-shock responseHSP20s-heat-shock proteinsmolecular crowdingPhyscomitrium patensproteomicsRNA-Seqthermotolerance

Identifiers

PMID33314263
PMCPMC8359368
OpenAlexW3112806644

What OpenQuestion holds

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LicenceCC BY-NC
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.