Evidence map›Paper›PMID 12011347›Full record

ArticlePlant physiology2002

LeCPK1, a calcium-dependent protein kinase from tomato. Plasma membrane targeting and biochemical characterization.

Frank Rutschmann, Urs Stalder, Markus Piotrowski, Claudia Oecking, Andreas Schaller

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

46 citing papers in PubMed, 104 citations in OpenAlex.

  1. International journal of molecular sciences · 2025
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  8. Review
  9. Proteins with calmodulin-like domains: structures and functional roles.Cellular and molecular life sciences : CMLS · 2019
    Review
  10. Targeted Profiling ofThe Plant cell · 2018
    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

5 authors at 3 institutions in 2 countries.

Frank RutschmannInstitute of Plant Sciences, Plant Biochemistry and Physiology Group, Swiss Federal Institute of Technology, Universitätstrasse 2, CH-8092 Zürich, Switzerland.
Urs Stalder
Markus Piotrowski
Claudia Oecking
Andreas Schaller
École Polytechnique Fédérale de Lausanne · CHRuhr University Bochum · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cDNA of LeCPK1, a calcium-dependent protein kinase, was cloned from tomato (Lycopersicon esculentum Mill.). LeCPK1 was expressed in Escherichia coli and purified from bacterial extracts. The recombinant protein was shown to be a functional protein kinase using a synthetic peptide as the substrate (syntide-2, Km = 85 microM). Autophosphorylation of LeCPK1 was observed on threonine and serine residues, one of which was identified as serine-439. Kinase activity was shown to be Ca2+ dependent and required the C-terminal, calmodulin-like domain of LeCPK1. Two classes of high- and low-affinity Ca2+-binding sites were observed, exhibiting dissociation constants of 0.6 and 55 microM, respectively. LeCPK1 was found to phosphorylate the regulatory C-terminal domain of the plasma membrane H+-ATPase in vitro. A potential role in the regulation of proton pump activity is corroborated by the apparent colocalization of the plasma membrane H+-ATPase and LeCPK1 in vivo. Upon transient expression in suspension-cultured cells, a C-terminal fusion of LeCPK1 with the green fluorescent protein was targeted to the plasma membrane. Myristoylation of the LeCPK1 N terminus was found to be required for plasma membrane targeting.

Indexed as

Amino Acid SequenceCalciumCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein KinasesCell MembraneCloning, MolecularGene Expression Regulation, EnzymologicGene Expression Regulation, PlantMolecular Sequence DataNicotianaPhosphorylationProtein KinasesProton-Translocating ATPasesSequence Homology, Amino AcidSolanum lycopersicumSubstrate SpecificityCalciumCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein KinasesProtein KinasesProton-Translocating ATPases

Identifiers

PMID12011347
PMCPMC155880
OpenAlexW2151284303

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.