Evidence map›Paper›PMID 23609608›Full record

ArticlePlant molecular biology2013

The myristoylated amino-terminus of an Arabidopsis calcium-dependent protein kinase mediates plasma membrane localization.

Sheen X Lu, Estelle M Hrabak

Open access · hybridAbstract read
In one paragraph

Article in Plant molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
8.8field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 63 citations in OpenAlex.

  1. Genome-wide analysis and expression profiling ofFrontiers in plant science · 2026
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  3. CPK28 is a modulator of purinergic signaling in plant growth and defense.The Plant journal : for cell and molecular biology · 2024
    Article
  4. Identification ofFrontiers in plant science · 2024
    Article
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  10. Frontiers in plant science · 2020
    Article
  11. Functional Analysis of theInternational journal of molecular sciences · 2018
    Article
  12. Targeted Profiling ofThe Plant cell · 2018
    Article
  13. Calcium-Dependent Protein Kinases in Phytohormone Signaling Pathways.International journal of molecular sciences · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors at 2 institutions in 1 country.

Sheen X LuDepartment of Molecular, Cellular & Biomedical Sciences, University of New Hampshire, Durham, NH 03824, USA.
Estelle M Hrabak
University of New Hampshire · USUniversity of New Hampshire at Manchester · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium-dependent protein kinases (CDPK) are a major group of calcium-stimulated kinases found in plants and some protists. Many CDPKs are membrane-associated, presumably because of lipid modifications at their amino termini. We investigated the subcellular location and myristoylation of AtCPK5, a member of the Arabidopsis CDPK family. Most AtCPK5 was associated with the plasma membrane as demonstrated by two-phase fractionation of plant microsomes and by in vivo detection of AtCPK5-GFP fusion proteins. AtCPK5 was a substrate for plant N-myristoyltransferase and myristoylation was prevented by converting the glycine at the proposed site of myristate attachment to alanine (G2A). In transgenic plants, a G2A mutation completely abolished AtCPK5 membrane association, indicating that myristoylation was essential for membrane binding. The first sixteen amino acids of AtCPK5 were sufficient to direct plasma membrane localization. In addition, differentially phosphorylated forms of AtCPK5 were detected both in planta and after expression of AtCPK5 in a cell-free plant extract. Our results demonstrate that AtCPK5 is myristoylated at its amino terminus and that myristoylation is required for membrane binding.

Indexed as

AcyltransferasesArabidopsisArabidopsis ProteinsBinding SitesCalciumCalcium-Calmodulin-Dependent Protein KinasesCell MembraneGreen Fluorescent ProteinsImmunoblottingMicroscopy, ConfocalMutationMyristic AcidPhosphorylationPlants, Genetically ModifiedProtein KinasesProtein TransportAcyltransferasesArabidopsis ProteinsCalciumCalcium-Calmodulin-Dependent Protein KinasesCPK5 protein, Arabidopsisglycylpeptide N-tetradecanoyltransferaseGreen Fluorescent ProteinsMyristic AcidProtein Kinases

Identifiers

PMID23609608
PMCPMC3668125
OpenAlexW1990502490

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.