Evidence map›Paper›PMID 26165835›Full record

ArticleOncogene2016

Opposing effects of pericentrin and microcephalin on the pericentriolar material regulate CHK1 activation in the DNA damage response.

A K Antonczak, L I Mullee, Y Wang, D Comartin, T Inoue, L Pelletier, C G Morrison

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Role of PLK4 inhibition in cancer therapy.Cancer metastasis reviews · 2025
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  19. Centrosomes in the DNA damage response--the hub outside the centre.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

7 authors at 3 institutions in 3 countries.

A K AntonczakCentre for Chromosome Biology, School of Natural Sciences, National University of Ireland Galway, Galway, Ireland.
L I MulleeCentre for Chromosome Biology, School of Natural Sciences, National University of Ireland Galway, Galway, Ireland.
Y WangCentre for Chromosome Biology, School of Natural Sciences, National University of Ireland Galway, Galway, Ireland.
D ComartinLunenfeld-Tanenbaum Research Institute, University of Toronto, Toronto, Canada.
T InoueDepartment of Cell Biology, Johns Hopkins University, Baltimore, MD, USA.
L PelletierLunenfeld-Tanenbaum Research Institute, University of Toronto, Toronto, Canada.
C G MorrisonCentre for Chromosome Biology, School of Natural Sciences, National University of Ireland Galway, Galway, Ireland.
Ollscoil na Gaillimhe – University of Galway · IEUniversity of Toronto · CAJohns Hopkins University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genotoxic stresses lead to centrosome amplification, a frequently-observed feature in cancer that may contribute to genome instability and to tumour cell invasion. Here we have explored how the centrosome controls DNA damage responses. For most of the cell cycle, centrosomes consist of two centrioles embedded in the proteinaceous pericentriolar material (PCM). Recent data indicate that the PCM is not an amorphous assembly of proteins, but actually a highly organised scaffold around the centrioles. The large coiled-coil protein, pericentrin, participates in PCM assembly and has been implicated in the control of DNA damage responses (DDRs) through its interactions with checkpoint kinase 1 (CHK1) and microcephalin (MCPH1). CHK1 is required for DNA damage-induced centrosome amplification, whereas MCPH1 deficiency greatly increases the amplification seen after DNA damage. We found that the PCM showed a marked expansion in volume and a noticeable change in higher-order organisation after ionising radiation treatment. PCM expansion was dependent on CHK1 kinase activity and was potentiated by MCPH1 deficiency. Furthermore, pericentrin deficiency or mutation of a separase cleavage site blocked DNA damage-induced PCM expansion. The extent of nuclear CHK1 activation after DNA damage reflected the level of PCM expansion, with a reduction in pericentrin-deficient or separase cleavage site mutant-expressing cells, and an increase in MCPH1-deficient cells that was suppressed by the loss of pericentrin. Deletion of the nuclear export signal of CHK1 led to its hyperphosphorylation after irradiation and reduced centrosome amplification. Deletion of the nuclear localisation signal led to low CHK1 activation and low centrosome amplification. From these data, we propose a feedback loop from the PCM to the nuclear DDR in which CHK1 regulates pericentrin-dependent PCM expansion to control its own activation.

Indexed as

DNA DamageAnimalsAntigensBinding SitesCell Cycle ProteinsCell Line, TumorCentriolesCentrosomeCheckpoint Kinase 1ChickensEnzyme ActivationFeedback, PhysiologicalGenes, ReporterMutationNeoplasm ProteinsNerve Tissue ProteinsAntigensCell Cycle ProteinsCheckpoint Kinase 1Neoplasm ProteinsNerve Tissue ProteinsNuclear Matrix-Associated ProteinspericentrinProtein KinasesRecombinant Fusion ProteinsSeparase

Identifiers

PMID26165835
OpenAlexW975657449

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.