Evidence map›Paper›PMID 25664600›Full record

ArticleCell cycle (Georgetown, Tex.)2015

Human Nek7-interactor RGS2 is required for mitotic spindle organization.

Edmarcia Elisa de Souza, Heidi Hehnly, Arina Marina Perez, Gabriela Vaz Meirelles, Juliana Helena Costa Smetana, Stephen Doxsey, Jörg Kobarg

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. In Mitosis You Are Not: The NIMA Family of Kinases inInternational journal of molecular sciences · 2022
    Review
  3. Article
  4. Article
  5. Checking NEKs: Overcoming a Bottleneck in Human Diseases.Molecules (Basel, Switzerland) · 2020
    Review
  6. Article
  7. Review
  8. Review
  9. 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

7 authors at 4 institutions in 2 countries.

Edmarcia Elisa de Souzaa Laboratório Nacional de Biociências-LNBio ; Centro Nacional de Pesquisa em Energia e Materiais-CNPEM ; Campinas , SP Brasil.
Heidi Hehnly
Arina Marina Perez
Gabriela Vaz Meirelles
Juliana Helena Costa Smetana
Stephen Doxsey
Jörg Kobarg
Brazilian Biosciences National Laboratory · BRBrazilian Center for Research in Energy and Materials · BRUniversity of Massachusetts Chan Medical School · USUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

Mitotic functions of cilia proteinsR01GM051994 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI DOXSEY, STEPHEN J · 1995 to 2014
$4.3M
Mother Centriole Appendages Regulate the AMIS Compartment and Cilogenesis.K99GM107355 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI HEHNLY, HEIDI · 2013 to 2014
$171k
NIGMS NIH HHS K99 GM107355NIGMS NIH HHS #NIH K99-GM107355NIGMS NIH HHS NIH RO1 GM051994-14
6 · The paper itself

Abstract

The mitotic spindle apparatus is composed of microtubule (MT) networks attached to kinetochores organized from 2 centrosomes (a.k.a. spindle poles). In addition to this central spindle apparatus, astral MTs assemble at the mitotic spindle pole and attach to the cell cortex to ensure appropriate spindle orientation. We propose that cell cycle-related kinase, Nek7, and its novel interacting protein RGS2, are involved in mitosis regulation and spindle formation. We found that RGS2 localizes to the mitotic spindle in a Nek7-dependent manner, and along with Nek7 contributes to spindle morphology and mitotic spindle pole integrity. RGS2-depletion leads to a mitotic-delay and severe defects in the chromosomes alignment and congression. Importantly, RGS2 or Nek7 depletion or even overexpression of wild-type or kinase-dead Nek7, reduced γ-tubulin from the mitotic spindle poles. In addition to causing a mitotic delay, RGS2 depletion induced mitotic spindle misorientation coinciding with astral MT-reduction. We propose that these phenotypes directly contribute to a failure in mitotic spindle alignment to the substratum. In conclusion, we suggest a molecular mechanism whereupon Nek7 and RGS2 may act cooperatively to ensure proper mitotic spindle organization.

Indexed as

Cloning, MolecularHumansImage Processing, Computer-AssistedMicroscopy, FluorescenceMitosisNIMA-Related KinasesPhosphorylationPlasmidsProtein Serine-Threonine KinasesRGS ProteinsSpindle ApparatusTime-Lapse ImagingTubulinTwo-Hybrid System TechniquesNEK7 protein, humanNIMA-Related KinasesProtein Serine-Threonine KinasesRGS2 protein, humanRGS ProteinsTubulincell divisionCREST, calcium-responsive transactivatorEB1, end-binding protein 1GAP, GTPase-activating proteinmitotic spindlemitotic spindle orientationMT, microtubuleNek7Nek, NIMA-related kinasePCM, centrosomal pericentriolar materialPD, pull-downPPI, protein-protein interactionRGS2RGS, regulators of G protein signalingshRNA, short-interfering RNAWB, Western blotting

Identifiers

PMID25664600
PMCPMC4614950
OpenAlexW2046027569

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.