Evidence map›Paper›PMID 32946374›Full record

ArticleeLife2020

WDR90 is a centriolar microtubule wall protein important for centriole architecture integrity.

Emmanuelle Steib, Marine H Laporte, Davide Gambarotto, Natacha Olieric, Celine Zheng, Susanne Borgers, Vincent Olieric, Maeva Le Guennec, France Koll, Anne-Marie Tassin and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 63 citations in OpenAlex.

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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

13 authors at 4 institutions in 3 countries.

Emmanuelle SteibUniversity of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.ORCID 0000-0002-5897-1964
Marine H LaporteUniversity of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.ORCID 0000-0002-7856-6763
Davide GambarottoUniversity of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.
Natacha OliericLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.
Celine ZhengLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.ORCID 0000-0002-8044-9371
Susanne BorgersUniversity of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.
Vincent OliericSwiss Light Source, Paul Scherrer Institut, Villigen, Switzerland.
Maeva Le GuennecUniversity of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.
France KollInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris Sud, Université Paris-Saclay, Gif sur Yvette, France.
Anne-Marie TassinInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris Sud, Université Paris-Saclay, Gif sur Yvette, France.
Michel O SteinmetzLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.
Paul GuichardUniversity of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.ORCID 0000-0002-0363-1049
Virginie HamelUniversity of Geneva, Department of Cell Biology, Sciences III, Geneva, Switzerland.ORCID 0000-0001-5092-2343
University of Geneva · CHPaul Scherrer Institute · CHCentre National de la Recherche Scientifique · FRUniversity of Basel · CH

Funding

European Research Council StG 715289Swiss National Science Foundation 31003A_166608Swiss National Science Foundation PP00P3_157517Swiss National Science Foundation PP00P3_187198
6 · The paper itself

Abstract

Centrioles are characterized by a nine-fold arrangement of microtubule triplets held together by an inner protein scaffold. These structurally robust organelles experience strenuous cellular processes such as cell division or ciliary beating while performing their function. However, the molecular mechanisms underlying the stability of microtubule triplets, as well as centriole architectural integrity remain poorly understood. Here, using ultrastructure expansion microscopy for nanoscale protein mapping, we reveal that POC16 and its human homolog WDR90 are components of the microtubule wall along the central core region of the centriole. We further found that WDR90 is an evolutionary microtubule associated protein. Finally, we demonstrate that WDR90 depletion impairs the localization of inner scaffold components, leading to centriole structural abnormalities in human cells. Altogether, this work highlights that WDR90 is an evolutionary conserved molecular player participating in centriole architecture integrity.

Indexed as

CentriolesCytoskeletal ProteinsMicrotubulesAnimalsCattleCell LineCells, CulturedChlamydomonasHumansPlant ProteinsCytoskeletal ProteinsPlant ProteinsWDR90 protein, humancell biologycentriolechlamydomonasexpansion microscopyhumaninner scaffoldmicrotubule

Identifiers

PMID32946374
PMCPMC7500955
OpenAlexW3087159146

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.