Evidence map›Paper›PMID 26023830›Full record

ArticleeLife2015

The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation.

Kacper B Rogala, Nicola J Dynes, Georgios N Hatzopoulos, Jun Yan, Sheng Kai Pong, Carol V Robinson, Charlotte M Deane, Pierre Gönczy, Ioannis Vakonakis

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

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  11. Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  12. Tracking of centriole inheritance inmicroPublication biology · 2020
    Article
  13. Review
  14. Article
  15. TheFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  16. Article
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  19. Mitotic Cell Division inGenetics · 2019
    Review
  20. Review
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

9 authors at 2 institutions in 2 countries.

Kacper B RogalaDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Nicola J DynesSwiss Institute for Experimental Cancer Research, School of Life Sciences, Swiss Federal Institute of Technology, Lausanne, Switzerland.
Georgios N HatzopoulosDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Jun YanDepartment of Chemistry, University of Oxford, Oxford, United Kingdom.
Sheng Kai PongSwiss Institute for Experimental Cancer Research, School of Life Sciences, Swiss Federal Institute of Technology, Lausanne, Switzerland.
Carol V RobinsonDepartment of Chemistry, University of Oxford, Oxford, United Kingdom.
Charlotte M DeaneDepartment of Statistics, University of Oxford, Oxford, United Kingdom.
Pierre GönczySwiss Institute for Experimental Cancer Research, School of Life Sciences, Swiss Federal Institute of Technology, Lausanne, Switzerland.
Ioannis VakonakisDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
University of Oxford · GBÉcole Polytechnique Fédérale de Lausanne · CH

Funding

Biotechnology and Biological Sciences Research Council BB/J008265/1European Research Council 268851Wellcome TrustWellcome Trust 088497/Z/09/Z
6 · The paper itself

Abstract

Centrioles are microtubule-based organelles crucial for cell division, sensing and motility. In Caenorhabditis elegans, the onset of centriole formation requires notably the proteins SAS-5 and SAS-6, which have functional equivalents across eukaryotic evolution. Whereas the molecular architecture of SAS-6 and its role in initiating centriole formation are well understood, the mechanisms by which SAS-5 and its relatives function is unclear. Here, we combine biophysical and structural analysis to uncover the architecture of SAS-5 and examine its functional implications in vivo. Our work reveals that two distinct self-associating domains are necessary to form higher-order oligomers of SAS-5: a trimeric coiled coil and a novel globular dimeric Implico domain. Disruption of either domain leads to centriole duplication failure in worm embryos, indicating that large SAS-5 assemblies are necessary for function in vivo.

Indexed as

Cell DivisionProtein MultimerizationAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell Cycle ProteinsCentriolesCrystallography, X-RayDNA Mutational AnalysisModels, MolecularProtein ConformationProtein Structure, TertiaryCaenorhabditis elegans ProteinsCell Cycle ProteinsSAS-5 protein, C elegansbiophysicsC. eleganscell biologycentriolescrystallographystructural biologystructures

Identifiers

PMID26023830
PMCPMC4471805
OpenAlexW2103166169

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.