Evidence map›Paper›PMID 19376835›Full record

ArticlePlant physiology2009

Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks.

Sonja Reiland, Gaëlle Messerli, Katja Baerenfaller, Bertran Gerrits, Anne Endler, Jonas Grossmann, Wilhelm Gruissem, Sacha Baginsky

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In one paragraph

Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 205 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
205citing papers in PubMed, 1 pooled it
17.2field-weighted citation impact, top 1% 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

205 citing papers in PubMed, 1 synthesis or guideline pooled it, 487 citations in OpenAlex.

  1. Pooled it
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  12. The Replicative DnaE Polymerase ofLife (Basel, Switzerland) · 2023
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  13. Article
  14. Redox Signaling in Plant Heat Stress Response.Antioxidants (Basel, Switzerland) · 2023
    Review
  15. Article
  16. Article
  17. The MAPK-Alfin-like 7 module negatively regulates ROS scavenging genes to promote NLR-mediated immunity.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Article
  20. Review

145 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

8 authors at 2 institutions in 1 country.

Sonja ReilandDepartment of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland.
Gaëlle Messerli
Katja Baerenfaller
Bertran Gerrits
Anne Endler
Jonas Grossmann
Wilhelm Gruissem
Sacha Baginsky
University of Zurich · CHETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have characterized the phosphoproteome of Arabidopsis (Arabidopsis thaliana) seedlings using high-accuracy mass spectrometry and report the identification of 1,429 phosphoproteins and 3,029 unique phosphopeptides. Among these, 174 proteins were chloroplast phosphoproteins. Motif-X (motif extractor) analysis of the phosphorylation sites in chloroplast proteins identified four significantly enriched kinase motifs, which include casein kinase II (CKII) and proline-directed kinase motifs, as well as two new motifs at the carboxyl terminus of ribosomal proteins. Using the phosphorylation motifs as a footprint for the activity of a specific kinase class, we connected the phosphoproteins with their putative kinases and constructed a chloroplast CKII phosphorylation network. The network topology suggests that CKII is a central regulator of different chloroplast functions. To provide insights into the dynamic regulation of protein phosphorylation, we analyzed the phosphoproteome at the end of day and end of night. The results revealed only minor changes in chloroplast kinase activities and phosphorylation site utilization. A notable exception was ATP synthase beta-subunit, which is found phosphorylated at CKII phosphorylation sites preferentially in the dark. We propose that ATP synthase is regulated in cooperation with 14-3-3 proteins by CKII-mediated phosphorylation of ATP synthase beta-subunit in the dark.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChloroplastsDatabases, ProteinModels, BiologicalMolecular Sequence DataPhosphoproteinsPhosphorylationProtein KinasesProteomeSequence AlignmentSubstrate SpecificityArabidopsis ProteinsPhosphoproteinsProtein KinasesProteome

Identifiers

PMID19376835
PMCPMC2689975
OpenAlexW2139750884

What OpenQuestion holds

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Registered trials

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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.