Evidence map›Paper›PMID 15659651›Full record

ArticleMolecular biology of the cell2005

Dynamic recruitment of Nek2 kinase to the centrosome involves microtubules, PCM-1, and localized proteasomal degradation.

Rebecca S Hames, Renarta E Crookes, Kees R Straatman, Andreas Merdes, Michelle J Hayes, Alison J Faragher, Andrew M Fry

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 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

61 citing papers in PubMed, 112 citations in OpenAlex.

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  12. In Mitosis You Are Not: The NIMA Family of Kinases inInternational journal of molecular sciences · 2022
    Review
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1 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

7 authors at 2 institutions in 1 country.

Rebecca S HamesDepartment of Biochemistry, University of Leicester, UK.
Renarta E Crookes
Kees R Straatman
Andreas Merdes
Michelle J Hayes
Alison J Faragher
Andrew M Fry
University of Leicester · GBWellcome Centre for Cell Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C000013/1Wellcome Trust
6 · The paper itself

Abstract

Centrosomes undergo dramatic changes in composition and activity during cell cycle progression. Yet mechanisms involved in recruiting centrosomal proteins are poorly understood. Nek2 is a cell cycle-regulated protein kinase required for regulation of centrosome structure at the G2/M transition. Here, we have addressed the processes involved in trafficking of Nek2 to the centrosome of human adult cells. We find that Nek2 exists in small, highly dynamic cytoplasmic particles that move to and from the centrosome. Many of these particles align along microtubules and a motif was identified in the Nek2 C-terminal noncatalytic domain that allows both microtubule binding and centrosome localization. FRAP experiments reveal that 70% of centrosomal Nek2 is rapidly turned over (t(1/2) approximately 3 s). Microtubules facilitate Nek2 trafficking to the centrosome but only over long distances. Cytoplasmic Nek2 particles colocalize in part with PCM-1 containing centriolar satellites and depletion of PCM-1 interferes with centrosomal recruitment of Nek2 and its substrate C-Nap1. Finally, we show that proteasomal degradation is necessary to allow rapid recruitment of new Nek2 molecules to the centrosome. Together, these data highlight multiple processes involved in regulating the abundance of Nek2 kinase at the centrosome including microtubule binding, the centriolar satellite component PCM-1, and localized protein degradation.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAutoantigensCell Cycle ProteinsCell Line, TumorCentrosomeCricetinaeHumansMicrotubulesMolecular Sequence DataNIMA-Related KinasesProteasome Endopeptidase ComplexProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryAutoantigensCell Cycle ProteinsNEK2 protein, humanNIMA-Related KinasesPCM1 protein, humanProteasome Endopeptidase ComplexProtein Serine-Threonine Kinases

Identifiers

PMID15659651
PMCPMC1073654
OpenAlexW2076027536

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.