Evidence map›Paper›PMID 16079175›Full record

ArticleMolecular biology of the cell2005

Active Nercc1 protein kinase concentrates at centrosomes early in mitosis and is necessary for proper spindle assembly.

Joan Roig, Aaron Groen, Jennifer Caldwell, Joseph Avruch

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Illumination of understudied ciliary kinases.Frontiers in molecular biosciences · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. In Mitosis You Are Not: The NIMA Family of Kinases inInternational journal of molecular sciences · 2022
    Review
  10. Review
  11. Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020
    Review
  12. Article
  13. Checking NEKs: Overcoming a Bottleneck in Human Diseases.Molecules (Basel, Switzerland) · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Mitotic Regulation by NEK Kinase Networks.Frontiers in cell and developmental biology · 2017
    Review
  18. Article
  19. Somatic Mutations in NEK9 Cause Nevus Comedonicus.American journal of human genetics · 2016
    Article
  20. Mitotic kinase cascades orchestrating timely disjunction and movement of centrosomes maintain chromosomal stability and prevent cancer.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2016
    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

4 authors at 1 institution in 1 country.

Joan RoigDepartment of Molecular Biology and Medical Services, Massachusetts General Hospital Harvard Medical School, Boston, MA 02114, USA. roig@molbio.mgh.harvard.edu
Aaron Groen
Jennifer Caldwell
Joseph Avruch
Harvard University · US

Funding

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 DK-17776NIDDK NIH HHS R37 DK017776
6 · The paper itself

Abstract

The Nercc1 protein kinase autoactivates in vitro and is activated in vivo during mitosis. Autoactivation in vitro requires phosphorylation of the activation loop at threonine 210. Mitotic activation of Nercc1 in mammalian cells is accompanied by Thr210 phosphorylation and involves a small fraction of total Nercc1. Mammalian Nercc1 coimmunoprecipitates gamma-tubulin and the activated Nercc1 polypeptides localize to the centrosomes and spindle poles during early mitosis, suggesting that active Nercc has important functions at the microtubular organizing center during cell division. To test this hypothesis, we characterized the Xenopus Nercc1 orthologue (XNercc). XNercc endogenous to meiotic egg extracts coprecipitates a multiprotein complex that contains gamma-tubulin and several components of the gamma-tubulin ring complex and localizes to the poles of spindles formed in vitro. Reciprocally, immunoprecipitates of the gamma-tubulin ring complex polypeptide Xgrip109 contain XNercc. Immunodepletion of XNercc from egg extracts results in delayed spindle assembly, fewer bipolar spindles, and the appearance of aberrant microtubule structures, aberrations corrected by addition of purified recombinant XNercc. XNercc immunodepletion also slows aster assembly induced by Ran-GTP, producing Ran-asters of abnormal size and morphology. Thus, Nercc1 contributes to both the centrosomal and the chromatin/Ran pathways that collaborate in the organization of a bipolar spindle.

Indexed as

Amino Acid SequenceAnimalsCell Line, TumorCentrosomeHumansIn Vitro TechniquesMitosisMolecular Sequence DataOocytesProtein BindingProtein Kinasesran GTP-Binding ProteinSpindle ApparatusTubulinXenopus laevisXenopus ProteinsNEK9 protein, XenopusProtein Kinasesran GTP-Binding ProteinTubulinXenopus Proteins

Identifiers

PMID16079175
PMCPMC1237086
OpenAlexW2115964608

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.