Evidence map›Paper›PMID 20062045›Full record

ArticleNature2010

Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons.

Valeria Specchia, Lucia Piacentini, Patrizia Tritto, Laura Fanti, Rosalba D'Alessandro, Gioacchino Palumbo, Sergio Pimpinelli, Maria P Bozzetti

Abstract read
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In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed
13.7field-weighted citation impact, top 1% 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

139 citing papers in PubMed, 268 citations in OpenAlex.

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79 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 1 country.

Valeria SpecchiaDipartimento di Scienze e Tecnologie Biologiche ed Ambientali (DiSTeBA), University of Salento, 73100 Lecce, Italy.
Lucia Piacentini
Patrizia Tritto
Laura Fanti
Rosalba D'Alessandro
Gioacchino Palumbo
Sergio Pimpinelli
Maria P Bozzetti
Istituto Pasteur · ITUniversity of Bari Aldo Moro · ITUniversity of Salento · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The canalization concept describes the resistance of a developmental process to phenotypic variation, regardless of genetic and environmental perturbations, owing to the existence of buffering mechanisms. Severe perturbations, which overcome such buffering mechanisms, produce altered phenotypes that can be heritable and can themselves be canalized by a genetic assimilation process. An important implication of this concept is that the buffering mechanism could be genetically controlled. Recent studies on Hsp90, a protein involved in several cellular processes and development pathways, indicate that it is a possible molecular mechanism for canalization and genetic assimilation. In both flies and plants, mutations in the Hsp90-encoding gene induce a wide range of phenotypic abnormalities, which have been interpreted as an increased sensitivity of different developmental pathways to hidden genetic variability. Thus, Hsp90 chaperone machinery may be an evolutionarily conserved buffering mechanism of phenotypic variance, which provides the genetic material for natural selection. Here we offer an additional, perhaps alternative, explanation for proposals of a concrete mechanism underlying canalization. We show that, in Drosophila, functional alterations of Hsp90 affect the Piwi-interacting RNA (piRNA; a class of germ-line-specific small RNAs) silencing mechanism leading to transposon activation and the induction of morphological mutants. This indicates that Hsp90 mutations can generate new variation by transposon-mediated 'canonical' mutagenesis.

Indexed as

Amino Acid SequenceAnimalsBenzoquinonesBlotting, SouthernDNA Transposable ElementsDrosophila melanogasterDrosophila ProteinsFemaleGene SilencingGenetic VariationGenotypeHeat-Shock ProteinsHomozygoteHSP90 Heat-Shock ProteinsLactams, MacrocyclicMaleBenzoquinonesDNA Transposable ElementsDrosophila ProteinsgeldanamycinHeat-Shock ProteinsHsp83 protein, DrosophilaHSP90 Heat-Shock ProteinsLactams, MacrocyclicMutant ProteinsProtein KinasesRNA, Small InterferingSte protein, Drosophila

Identifiers

PMID20062045
OpenAlexW1976854735

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.