Evidence map›Paper›PMID 21358806›Full record

ArticlePloS one2011

Oocyte-targeted deletion reveals that hsp90b1 is needed for the completion of first mitosis in mouse zygotes.

Christophe Audouard, Florent Le Masson, Colette Charry, Zihai Li, Elisabeth S Christians

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 37 citations in OpenAlex.

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  5. [High-resolution Differential Proteomic Analysis of Mouse Secondary Oocytes and First Polar Bodies].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2025
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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.

Christophe AudouardCentre de Biologie du Développement, Université Toulouse 3-Paul Sabatier, UPS, UMR 5547, Toulouse, France.
Florent Le Masson
Colette Charry
Zihai Li
Elisabeth S Christians
Centre de Biologie du Développement · FRMedical University of South Carolina · US

Funding

Roles and Mechanisms of gp96 in Chaperoning Innate ImmunityR01AI070603 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI LI, ZIHAI · 2007 to 2016
$3.8M
NIAID NIH HHS R01 AI070603NIAID NIH HHS R01AI070603
6 · The paper itself

Abstract

backgroundHsp90b1 is an endoplasmic reticulum (ER) chaperone (also named Grp94, ERp99, gp96,Targ2, Tra-1, Tra1, Hspc4) (MGI:98817) contributing with Hspa5 (also named Grp78, BIP) (MGI:95835) to protein folding in ER compartment. Besides its high protein expression in mouse oocytes, little is known about Hsp90b1 during the transition from oocyte-to-embryo. Because the constitutive knockout of Hsp90b1 is responsible for peri-implantation embryonic lethality, it was not yet known whether Hsp90b1 is a functionally important maternal factor. METHODOLOGY/

findingsTo circumvent embryonic lethality, we established an oocyte-specific conditional knockout line taking advantage of the more recently created floxed Hsp90b1 line (Hsp90b1(flox), MGI:3700023) in combination with the transgenic mouse line expressing the cre recombinase under the control of zona pellucida 3 (ZP3) promoter (Zp3-cre, MGI:2176187). Altered expression of Hsp90b1 in growing oocytes provoked a limited, albeit significant reduction of the zona pellucida thickness but no obvious anomalies in follicular growth, meiotic maturation or fertilization. Interestingly, mutant zygotes obtained from oocytes lacking Hsp90b1 were unable to reach the 2-cell stage. They exhibited either a G2/M block or, more frequently an abnormal mitotic spindle leading to developmental arrest. Despite the fact that Hspa5 displayed a similar profile of expression as Hsp90b1, we found that HSPA5 and HSP90B1 did not fully colocalize in zygotes suggesting distinct function for the two chaperones. Consequently, even if HSPA5 was overexpressed in Hsp90b1 mutant embryos, it did not compensate for HSP90B1 deficiency. Finally, further characterization of ER compartment and cytoskeleton revealed a defective organization of the cytoplasmic region surrounding the mutant zygotic spindle.

conclusionsOur findings demonstrate that the maternal contribution of Hsp90b1 is critical for the development of murine zygotes. All together our data indicate that Hsp90b1 is involved in unique and specific aspects of the first mitosis, which brings together the maternal and paternal genomes on a single spindle.

Indexed as

AnimalsAnimals, NewbornCells, CulturedEmbryo, MammalianEndoplasmic Reticulum Chaperone BiPFemaleGene DeletionGene Expression Regulation, DevelopmentalHSP90 Heat-Shock ProteinsMiceMice, TransgenicMitosisModels, BiologicalMutagenesis, Site-DirectedOocytesOogenesisEndoplasmic Reticulum Chaperone BiPHsp90b1 protein, mouseHSP90 Heat-Shock ProteinsHspa5 protein, mouse

Identifiers

PMID21358806
PMCPMC3039677
OpenAlexW2168032141

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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.