Evidence map›Paper›PMID 16807317›Full record

ArticleNucleic acids research2006

Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis proteins involved in RNA metabolism.

Sergio de la Fuente van Bentem, Dorothea Anrather, Elisabeth Roitinger, Armin Djamei, Thomas Hufnagl, Andrea Barta, Edina Csaszar, Ilse Dohnal, David Lecourieux, Heribert Hirt

Open access · goldAbstract readEvaluation Study
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

60 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
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  3. Article
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  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Dynamics of Protein Phosphorylation duringInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. Purification and Biochemical Characterization ofInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
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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

10 authors at 1 institution in 1 country.

Sergio de la Fuente van BentemDepartment of Plant Molecular Biology, Max F. Perutz Laboratories, University of Vienna, Dr Bohr-Gasse 9, 1030 Vienna, Austria. sergio.de.la.fuente.van.bentem@univie.ac.at
Dorothea Anrather
Elisabeth Roitinger
Armin Djamei
Thomas Hufnagl
Andrea Barta
Edina Csaszar
Ilse Dohnal
David Lecourieux
Heribert Hirt
Max Perutz Labs · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most regulatory pathways are governed by the reversible phosphorylation of proteins. Recent developments in mass spectrometry-based technology allow the large-scale analysis of protein phosphorylation. Here, we show the application of immobilized metal affinity chromatography to purify phosphopeptides from Arabidopsis extracts. Phosphopeptide sequences were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS/MS). A total of 79 unique phosphorylation sites were determined in 22 phosphoproteins with a putative role in RNA metabolism, including splicing of mRNAs. Among these phosphoproteins, 12 Ser/Arg-rich (SR) splicing factors were identified. A conserved phosphorylation site was found in most of the phosphoproteins, including the SR proteins, suggesting that these proteins are targeted by the same or a highly related protein kinase. To test this hypothesis, Arabidopsis SR protein-specific kinase 4 (SRPK4) that was initially identified as an interactor of SR proteins was tested for its ability to phosphorylate the SR protein RSp31. In vitro kinase assays showed that all in vivo phosphorylation sites of RSp31 were targeted by SRPK4. These data suggest that the plant mRNA splicing machinery is a major target of phosphorylation and that a considerable number of proteins involved in RNA metabolism may be targeted by SRPKs.

Indexed as

RNA SplicingAmino Acid MotifsAmino Acid SequenceArabidopsisArabidopsis ProteinsCell NucleusChromatography, AffinityCytosolMass SpectrometryMolecular Sequence DataPhosphopeptidesPhosphoproteinsPhosphorylationProtein IsoformsProtein Serine-Threonine KinasesProteomicsArabidopsis ProteinsPhosphopeptidesPhosphoproteinsProtein IsoformsProtein Serine-Threonine KinasesRNA-Binding ProteinsRNA, MessengerRNA, PlantRSp31 protein, ArabidopsisSerine-Arginine Splicing Factors

Identifiers

PMID16807317
PMCPMC1904105
OpenAlexW2120261223

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.