Evidence map›Paper›PMID 25930153›Full record

ArticleProteomics2015

Label-free quantitative analysis of the casein kinase 2-responsive phosphoproteome of the marine minimal model species Ostreococcus tauri.

Thierry Le Bihan, Matthew Hindle, Sarah F Martin, Martin E Barrios-Llerena, Johanna Krahmer, Katalin Kis, Andrew J Millar, Gerben van Ooijen

Open access · hybridAbstract read
In one paragraph

Article in Proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Thierry Le BihanSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Matthew HindleSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Sarah F MartinSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Martin E Barrios-LlerenaSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Johanna KrahmerSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Katalin KisSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Andrew J MillarSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Gerben van OoijenSchool of Biological Sciences, University of Edinburgh, Edinburgh, UK.
University of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D019621Biotechnology and Biological Sciences Research Council BB/D019621/1Biotechnology and Biological Sciences Research Council BB/ J009423Biotechnology and Biological Sciences Research Council BB/J009423/1Wellcome Trust 096995
6 · The paper itself

Abstract

Casein kinase 2 (CK2) is a protein kinase that phosphorylates a plethora of cellular target proteins involved in processes including DNA repair, cell cycle control, and circadian timekeeping. CK2 is functionally conserved across eukaryotes, although the substrate proteins identified in a range of complex tissues are often different. The marine alga Ostreococcus tauri is a unicellular eukaryotic model organism ideally suited to efficiently study generic roles of CK2 in the cellular circadian clock. Overexpression of CK2 leads to a slow circadian rhythm, verifying functional conservation of CK2 in timekeeping. The proteome was analysed in wild-type and CK2-overexpressing algae at dawn and dusk, revealing that differential abundance of the global proteome across the day is largely unaffected by overexpression. However, CK2 activity contributed more strongly to timekeeping at dusk than at dawn. The phosphoproteome of a CK2 overexpression line and cells treated with CK2 inhibitor was therefore analysed and compared to control cells at dusk. We report an extensive catalogue of 447 unique CK2-responsive differential phosphopeptide motifs to inform future studies into CK2 activity in the circadian clock of more complex tissues. All MS data have been deposited in the ProteomeXchange with identifier PXD000975 (http://proteomecentral.proteomexchange.org/dataset/PXD000975).

Indexed as

Casein Kinase IIChlorophytaGene Expression Regulation, PlantPlant ProteinsProteomeCasein Kinase IIPlant ProteinsProteomeCasein kinase 2Cell biologyCircadian clockMarine algaeOstreococcus tauriPhosphoproteomics

Identifiers

PMID25930153
PMCPMC4716292
OpenAlexW2006186207

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.