Evidence map›Paper›PMID 25093993›Full record

ArticleJournal of proteome research2014

Characterization of the human NEK7 interactome suggests catalytic and regulatory properties distinct from those of NEK6.

Edmarcia Elisa de Souza, Gabriela Vaz Meirelles, Bárbara Biatriz Godoy, Arina Marina Perez, Juliana Helena Costa Smetana, Stephen J Doxsey, Mark E McComb, Catherine E Costello, Stephen A Whelan, Jörg Kobarg

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 20% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.

  1. Pooled it
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  15. Checking NEKs: Overcoming a Bottleneck in Human Diseases.Molecules (Basel, Switzerland) · 2020
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. GBS Mapping and Analysis of Genes Conserved betweenInternational journal of molecular sciences · 2018
    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

10 authors at 4 institutions in 2 countries.

Edmarcia Elisa de SouzaLaboratório Nacional de Biociências, Centro Nacional de Pesquisa em Energia e Materiais , Campinas, São Paulo, Brazil.
Gabriela Vaz Meirelles
Bárbara Biatriz Godoy
Arina Marina Perez
Juliana Helena Costa Smetana
Stephen J Doxsey
Mark E McComb
Catherine E Costello
Stephen A Whelan
Jörg Kobarg
Boston University · USBrazilian Biosciences National Laboratory · BRBrazilian Center for Research in Energy and Materials · BRUniversity of Massachusetts Chan Medical School · US

Funding

Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
NHLBI NIH HHS HHSN268201000031CNIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

Human NEK7 is a regulator of cell division and plays an important role in growth and survival of mammalian cells. Human NEK6 and NEK7 are closely related, consisting of a conserved C-terminal catalytic domain and a nonconserved and disordered N-terminal regulatory domain, crucial to mediate the interactions with their respective proteins. Here, in order to better understand NEK7 cellular functions, we characterize the NEK7 interactome by two screening approaches: one using a yeast two-hybrid system and the other based on immunoprecipitation followed by mass spectrometry analysis. These approaches led to the identification of 61 NEK7 interactors that contribute to a variety of biological processes, including cell division. Combining additional interaction and phosphorylation assays from yeast two-hybrid screens, we validated CC2D1A, TUBB2B, MNAT1, and NEK9 proteins as potential NEK7 interactors and substrates. Notably, endogenous RGS2, TUBB, MNAT1, NEK9, and PLEKHA8 localized with NEK7 at key sites throughout the cell cycle, especially during mitosis and cytokinesis. Furthermore, we obtained evidence that the closely related kinases NEK6 and NEK7 do not share common interactors, with the exception of NEK9, and display different modes of protein interaction, depending on their N- and C-terminal regions, in distinct fashions. In summary, our work shows for the first time a comprehensive NEK7 interactome that, combined with functional in vitro and in vivo assays, suggests that NEK7 is a multifunctional kinase acting in different cellular processes in concert with cell division signaling and independently of NEK6.

Indexed as

Cell CycleHumansImmunoprecipitationMass SpectrometryNIMA-Related KinasesProtein BindingProtein Interaction MapsProtein Serine-Threonine KinasesProteomicsTwo-Hybrid System TechniquesNEK6 protein, humanNEK7 protein, humanNIMA-Related KinasesProtein Serine-Threonine Kinases

Identifiers

PMID25093993
PMCPMC4156247
OpenAlexW2058753428

What OpenQuestion holds

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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.