Evidence map›Paper›PMID 34654813›Full record

ArticleNature communications2021

Sub-centrosomal mapping identifies augmin-γTuRC as part of a centriole-stabilizing scaffold.

Nina Schweizer, Laurence Haren, Ilaria Dutto, Ricardo Viais, Cristina Lacasa, Andreas Merdes, Jens Lüders

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.8field-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

31 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  3. The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026
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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

7 authors at 2 institutions in 2 countries.

Nina SchweizerMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), 08028, Barcelona, Spain.ORCID 0000-0001-5970-3921
Laurence HarenMolecular, Cellular and Developmental Biology, Centre de Biologie Intégrative, CNRS-Université Toulouse III, 31062, Toulouse, France.ORCID 0000-0002-2645-5308
Ilaria DuttoMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), 08028, Barcelona, Spain.
Ricardo ViaisMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), 08028, Barcelona, Spain.ORCID 0000-0002-8146-3693
Cristina LacasaMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), 08028, Barcelona, Spain.
Andreas MerdesMolecular, Cellular and Developmental Biology, Centre de Biologie Intégrative, CNRS-Université Toulouse III, 31062, Toulouse, France.ORCID 0000-0002-3739-2728
Jens LüdersMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), 08028, Barcelona, Spain. jens.luders@irbbarcelona.org.ORCID 0000-0002-9018-7977
Institute for Research in Biomedicine · ESCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Centriole biogenesis and maintenance are crucial for cells to generate cilia and assemble centrosomes that function as microtubule organizing centers (MTOCs). Centriole biogenesis and MTOC function both require the microtubule nucleator γ-tubulin ring complex (γTuRC). It is widely accepted that γTuRC nucleates microtubules from the pericentriolar material that is associated with the proximal part of centrioles. However, γTuRC also localizes more distally and in the centriole lumen, but the significance of these findings is unclear. Here we identify spatially and functionally distinct subpopulations of centrosomal γTuRC. Luminal localization is mediated by augmin, which is linked to the centriole inner scaffold through POC5. Disruption of luminal localization impairs centriole integrity and interferes with cilium assembly. Defective ciliogenesis is also observed in γTuRC mutant fibroblasts from a patient suffering from microcephaly with chorioretinopathy. These results identify a non-canonical role of augmin-γTuRC in the centriole lumen that is linked to human disease.

Indexed as

AnimalsCarrier ProteinsCell Cycle ProteinsCell LineCentriolesCentrosomeCiliaFemaleHumansMaleMiceMicrotubule-Associated ProteinsMicrotubule-Organizing CenterMicrotubulesNeuronsaugmin protein, humanCarrier ProteinsCell Cycle ProteinsMicrotubule-Associated ProteinsPOC5 protein, human

Identifiers

PMID34654813
PMCPMC8519919
OpenAlexW3207344627

What OpenQuestion holds

Textmetadata
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.