Evidence map›Paper›PMID 21642957›Full record

ArticleThe EMBO journal2011

Nek9 is a Plk1-activated kinase that controls early centrosome separation through Nek6/7 and Eg5.

M Teresa Bertran, Sara Sdelci, Laura Regué, Joseph Avruch, Carme Caelles, Joan Roig

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

115 citing papers in PubMed, 191 citations in OpenAlex.

  1. Review
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  15. The NIMA-related kinase family and cancer.Frontiers in oncology · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. KIF11 UFMylation Maintains Photoreceptor Cilium Integrity and Retinal Homeostasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  20. Review

55 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

M Teresa BertranCell Signalling Research Group, Molecular Medicine Program, Institute for Research in Biomedicine (IRB Barcelona), Barcelona, Spain.
Sara Sdelci
Laura Regué
Joseph Avruch
Carme Caelles
Joan Roig
Institute for Research in Biomedicine · ESHarvard University · US

Funding

Pilot & Feasibility ProgramP30DK043351 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI RAYMOND T CHUNG · 1991 to 2026
$35.3M
PHOSPHOPEPTIDE METABOLISM IN ADIPOCYTESR37DK017776 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI AVRUCH, JOSEPH · 1999 to 2018
$9.3M
PHOSPHOPEPTIDE METABOLISM IN ADIPOCYTESR01DK017776 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI AVRUCH, JOSEPH · 1986 to 1998
–
NIDDK NIH HHS DK17776NIDDK NIH HHS P30 DK043351NIDDK NIH HHS R37 DK017776
6 · The paper itself

Abstract

The NIMA-family kinases Nek9/Nercc1, Nek6 and Nek7 form a signalling module required for mitotic spindle assembly. Nek9, the upstream kinase, is activated during prophase at centrosomes although the details of this have remained elusive. We now identify Plk1 as Nek9 direct activator and propose a two-step activation mechanism that involves Nek9 sequential phosphorylation by CDK1 and Plk1. Furthermore, we show that Plk1 controls prophase centrosome separation through the activation of Nek9 and ultimately the phosphorylation of the mitotic kinesin Eg5 at Ser1033, a Nek6/7 site that together with the CDK1 site Thr926 we establish contributes to the accumulation of Eg5 at centrosomes and is necessary for subsequent centrosome separation and timely mitosis. Our results provide a basis to understand signalling downstream of Plk1 and shed light on the role of Eg5, Plk1 and the NIMA-family kinases in the control of centrosome separation and normal mitotic progression.

Indexed as

Cell CycleCell Cycle ProteinsCells, CulturedCentrosomeEnzyme ActivationGene Knockdown TechniquesHeLa CellsHumansKinesinsMitosisNIMA-Related KinasesPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, Small InterferingCell Cycle ProteinsKIF11 protein, humanKinesinsNEK6 protein, humanNEK7 protein, humanNEK9 protein, humanNIMA-Related KinasesPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, Small Interfering

Identifiers

PMID21642957
PMCPMC3155310
OpenAlexW2118639465

What OpenQuestion holds

Textmetadata
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.