Evidence map›Paper›PMID 39543170›Full record

ArticleNature communications2024

An interaction network of inner centriole proteins organised by POC1A-POC1B heterodimer crosslinks ensures centriolar integrity.

Cornelia Sala, Martin Würtz, Enrico Salvatore Atorino, Annett Neuner, Patrick Partscht, Thomas Hoffmann, Sebastian Eustermann, Elmar Schiebel

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Centriolar Protein POC5 Regulates Human Adipogenesis and Cellular Senescence: Insights From a Novel Metabolic Ciliopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Review
  3. Review
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  6. The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
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  14. Article
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.

Cornelia SalaZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ)-ZMBH Allianz, Universität Heidelberg, Heidelberg, Germany.ORCID 0009-0007-4351-6401
Martin Würtz *Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ)-ZMBH Allianz, Universität Heidelberg, Heidelberg, Germany.ORCID 0000-0002-4504-4723
Enrico Salvatore Atorino *European Molecular Biology Laboratory (EMBL) Heidelberg, Heidelberg, Germany.
Annett NeunerZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ)-ZMBH Allianz, Universität Heidelberg, Heidelberg, Germany.
Patrick PartschtGerman Cancer Research Center (DKFZ), Heidelberg, Germany.ORCID 0000-0002-8766-3901
Thomas HoffmannEuropean Molecular Biology Laboratory (EMBL) Heidelberg, Heidelberg, Germany.ORCID 0000-0002-2980-8324
Sebastian EustermannEuropean Molecular Biology Laboratory (EMBL) Heidelberg, Heidelberg, Germany.ORCID 0000-0002-4439-7770
Elmar SchiebelZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ)-ZMBH Allianz, Universität Heidelberg, Heidelberg, Germany. e.schiebel@zmbh.uni-heidelberg.de.ORCID 0000-0002-3683-247X

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) Schi295/8-2
6 · The paper itself

Abstract

Centriole integrity, vital for cilia formation and chromosome segregation, is crucial for human health. The inner scaffold within the centriole lumen composed of the proteins POC1B, POC5 and FAM161A is key to this integrity. Here, we provide an understanding of the function of inner scaffold proteins. We demonstrate the importance of an interaction network organised by POC1A-POC1B heterodimers within the centriole lumen, where the WD40 domain of POC1B localises close to the centriole wall, while the POC5-interacting WD40 of POC1A resides in the centriole lumen. The POC1A-POC5 interaction and POC5 tetramerization are essential for inner scaffold formation and centriole stability. The microtubule binding proteins FAM161A and MDM1 by binding to POC1A-POC1B, likely positioning the POC5 tetramer near the centriole wall. Disruption of POC1A or POC1B leads to centriole microtubule defects and deletion of both genes causes centriole disintegration. These findings provide insights into organisation and function of the inner scaffold.

Indexed as

Cell Cycle ProteinsCentriolesHumansMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein Interaction MapsProtein MultimerizationCell Cycle ProteinsMicrotubule-Associated Proteins

Identifiers

PMID39543170
PMCPMC11564547

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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.