Evidence map›Paper›PMID 21219905›Full record

ArticleFEBS letters2011

Protein N-acylation overrides differing targeting signals.

Simon Stael, Roman G Bayer, Norbert Mehlmer, Markus Teige

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Chloroplast Calcium Signaling in the Spotlight.Frontiers in plant science · 2020
    Review
  6. TheInternational journal of molecular sciences · 2018
    Review
  7. Article
  8. Targeted Profiling ofThe Plant cell · 2018
    Article
  9. Calcium-Dependent Protein Kinases in Phytohormone Signaling Pathways.International journal of molecular sciences · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. CDPKs in immune and stress signaling.Trends in plant science · 2013
    Review
  20. 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

4 authors at 1 institution in 1 country.

Simon Stael *Department of Biochemistry and Cell Biology, MFPL, University of Vienna. Dr. Bohrgasse 9, A-1030 Vienna, Austria.
Roman G Bayer *Department of Biochemistry and Cell Biology, MFPL, University of Vienna. Dr. Bohrgasse 9, A-1030 Vienna, Austria.
Norbert MehlmerDepartment of Biochemistry and Cell Biology, MFPL, University of Vienna. Dr. Bohrgasse 9, A-1030 Vienna, Austria.
Markus TeigeDepartment of Biochemistry and Cell Biology, MFPL, University of Vienna. Dr. Bohrgasse 9, A-1030 Vienna, Austria.
University of Vienna · AT

Funding

Austrian Science Fund FWF I 253
6 · The paper itself

Abstract

In a bioinformatics based screen for chloroplast-localized protein kinases we noticed that available protein targeting predictors falsely predicted chloroplast localization. This seems to be due to interference with N-terminal protein acylation, which is of particular importance for protein kinases. Their N-myristoylation was found to be highly overrepresented in the proteome, whereas myristoylation motifs are almost absent in known chloroplast proteins. However, only abolishing their myristoylation was not sufficient to target those kinases to chloroplasts and resulted in nuclear accumulation instead. In contrast, inhibition of N-myristoylation of a calcium-dependent protein kinase was sufficient to alter its localization from the plasma membrane to chloroplasts and chloroplast localization of ferredoxin-NADP+ reductase and Rubisco activase could be efficiently suppressed by artificial introduction of myristoylation and palmitoylation sites.

Indexed as

Protein TransportAcylationArabidopsis ProteinsCalcium-Calmodulin-Dependent Protein KinasesCell MembraneChloroplastsFerredoxin-NADP ReductaseLipoylationMutant ProteinsMyristic AcidNicotianaPalmitic AcidPlant ProteinsProtein KinasesProtein Processing, Post-TranslationalRecombinant Fusion ProteinsArabidopsis ProteinsCalcium-Calmodulin-Dependent Protein KinasesFerredoxin-NADP ReductaseMutant ProteinsMyristic AcidPalmitic AcidPlant ProteinsProtein Kinasesrca protein, plantRecombinant Fusion Proteins

Identifiers

PMID21219905
PMCPMC3971372
OpenAlexW2171550550

What OpenQuestion holds

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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.