Evidence map›Paper›PMID 24590172›Full record

ArticleThe Journal of cell biology2014

Mechanisms of HsSAS-6 assembly promoting centriole formation in human cells.

Debora Keller, Meritxell Orpinell, Nicolas Olivier, Malte Wachsmuth, Robert Mahen, Romain Wyss, Virginie Hachet, Jan Ellenberg, Suliana Manley, Pierre Gönczy

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 83 citations in OpenAlex.

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  8. The E3 ligase Poe promotes Pericentrin degradation.Molecular biology of the cell · 2023
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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

10 authors at 3 institutions in 2 countries.

Debora KellerSwiss Institute for Experimental Cancer Research, School of Life Sciences, 2 Laboratory for Experimental Biophysics, and 3 Institute for Science and Chemical Engineering, Swiss Federal Institute of Technology, 1015 Lausanne, Switzerland.
Meritxell Orpinell
Nicolas Olivier
Malte Wachsmuth
Robert Mahen
Romain Wyss
Virginie Hachet
Jan Ellenberg
Suliana Manley
Pierre Gönczy
Swiss Group For Clinical Cancer Research · CHÉcole Polytechnique Fédérale de Lausanne · CHEuropean Molecular Biology Laboratory · DE

Funding

Wellcome Trust 100090
6 · The paper itself

Abstract

SAS-6 proteins are thought to impart the ninefold symmetry of centrioles, but the mechanisms by which their assembly occurs within cells remain elusive. In this paper, we provide evidence that the N-terminal, coiled-coil, and C-terminal domains of HsSAS-6 are each required for procentriole formation in human cells. Moreover, the coiled coil is necessary and sufficient to mediate HsSAS-6 centrosomal targeting. High-resolution imaging reveals that GFP-tagged HsSAS-6 variants localize in a torus around the base of the parental centriole before S phase, perhaps indicative of an initial loading platform. Moreover, fluorescence recovery after photobleaching analysis demonstrates that HsSAS-6 is immobilized progressively at centrosomes during cell cycle progression. Using fluorescence correlation spectroscopy and three-dimensional stochastic optical reconstruction microscopy, we uncover that HsSAS-6 is present in the cytoplasm primarily as a homodimer and that its oligomerization into a ninefold symmetrical ring occurs at centrioles. Together, our findings lead us to propose a mechanism whereby HsSAS-6 homodimers are targeted to centrosomes where the local environment and high concentration of HsSAS-6 promote oligomerization, thus initiating procentriole formation.

Indexed as

Cell CycleCell Cycle ProteinsCell Line, TumorCentriolesDimerizationFluorescence Recovery After PhotobleachingHumansModels, BiologicalProtein TransportCell Cycle ProteinsSASS6 protein, human

Identifiers

PMID24590172
PMCPMC3941056
OpenAlexW2098444562

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.