Evidence map›Paper›PMID 20118232›Full record

ArticleThe Journal of biological chemistry2010

Tobacco calcium-dependent protein kinases are differentially phosphorylated in vivo as part of a kinase cascade that regulates stress response.

Claus-Peter Witte, Nana Keinath, Ullrich Dubiella, Raphael Demoulière, Anindita Seal, Tina Romeis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
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  5. Review
  6. Article
  7. Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. PROTEIN PHOSPHATASE 2A-B'Plant physiology · 2020
    Article
  10. Article
  11. Targeted Profiling ofThe Plant cell · 2018
    Article
  12. Article
  13. Calcium-Dependent Protein Kinases in Phytohormone Signaling Pathways.International journal of molecular sciences · 2017
    Review
  14. Article
  15. Article
  16. 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

6 authors at 4 institutions in 2 countries.

Claus-Peter WitteDepartment of Plant Biochemistry, Institute for Biology, Freie Universität Berlin, Königin-Luise-Strasse 12-16, 14195 Berlin, Germany.
Nana KeinathDepartment of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50935 Cologne, Germany.
Ullrich DubiellaDepartment of Plant Biochemistry, Institute for Biology, Freie Universität Berlin, Königin-Luise-Strasse 12-16, 14195 Berlin, Germany.
Raphael DemoulièreDepartment of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50935 Cologne, Germany.
Anindita SealDepartment of Biotechnology, West Bengal University of Technology BF-142, Sector I, Salt Lake, Calcutta 700064, India.
Tina RomeisDepartment of Plant Biochemistry, Institute for Biology, Freie Universität Berlin, Königin-Luise-Strasse 12-16, 14195 Berlin, Germany. Electronic address: romeis@zedat.fu-berlin.de.
Freie Universität Berlin · DEMax Planck Institute for Plant Breeding Research · DEMaulana Abul Kalam Azad University of Technology, West Bengal · INMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vivo phosphorylation sites of the tobacco calcium-dependent protein kinases NtCDPK2 and NtCDPK3 were determined in response to biotic or abiotic stress. Stress-inducible phosphorylation was exclusively located in the variable N termini, where both kinases were phosphorylated differentially despite 91% overall sequence identity. In NtCDPK2, serine 40 and threonine 65 were phosphorylated within 2 min after stress. Whereas Thr(65) is subjected to intra-molecular in vivo autophosphorylation, Ser(40) represents a target for a regulatory upstream protein kinase, and correct NtCDPK2 membrane localization is required for Ser(40) phosphorylation. NtCDPK3 is phosphorylated at least at two sites in the N terminus by upstream kinase(s) upon stress stimulus, first at Ser(54), a site not present in NtCDPK2, and also at a second undetermined site not identical to Ser(40). Domain swap experiments established that differential phosphorylation of both kinases is exclusively determined by the respective N termini. A cell death-inducing response was only observed upon expression of a truncated variant lacking the junction and calcium-binding domain of NtCDPK2 (VK2). This response required protein kinase activity and was reduced when subcellular membrane localization was disturbed by a mutation in the myristoylation and palmitoylation site. Our data indicate that CDPKs are integrated in stress-dependent protein kinase signaling cascades, and regulation of CDPK function in response to in vivo stimulation is dependent on its membrane localization.

Indexed as

Gene Expression Regulation, EnzymologicGene Expression Regulation, PlantAmino Acid SequenceArabidopsisCalciumCalcium-Calmodulin-Dependent Protein KinasesKineticsMass SpectrometryMolecular Sequence DataMutagenesis, Site-DirectedNicotianaPhenotypePhosphorylationProtein KinasesSequence Homology, Amino AcidSignal TransductionCalciumCalcium-Calmodulin-Dependent Protein KinasesProtein Kinases

Identifiers

PMID20118232
PMCPMC2843223
OpenAlexW2087122633

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.