Evidence map›Paper›PMID 15247393›Full record

ArticlePlant physiology2004

Autophosphorylation and subcellular localization dynamics of a salt- and water deficit-induced calcium-dependent protein kinase from ice plant.

E Wassim Chehab, O Rahul Patharkar, Adrian D Hegeman, Tahar Taybi, John C Cushman

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
  4. CaInternational journal of molecular sciences · 2021
    Article
  5. Review
  6. Article
  7. TheInternational journal of molecular sciences · 2018
    Review
  8. Article
  9. Article
  10. Article
  11. Autophosphorylation-based Calcium (CaThe Journal of biological chemistry · 2017
    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

5 authors at 3 institutions in 2 countries.

E Wassim ChehabDepartment of Biochemistry/MS200, University of Nevada, Reno, Nevada 89557-0014, USA.
O Rahul Patharkar
Adrian D Hegeman
Tahar Taybi
John C Cushman
Newcastle University · GBUniversity of Nevada, Reno · USMassachusetts General Hospital · US

Funding

Calcium Dependent Protein Kinase AutophosphorylationF32GM069315 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI HEGEMAN, ADRIAN D · 2003 to 2004
$95k
NIGMS NIH HHS F32 GM069315
6 · The paper itself

Abstract

A salinity and dehydration stress-responsive calcium-dependent protein kinase (CDPK) was isolated from the common ice plant (Mesembryanthemum crystallinum; McCPK1). McCPK1 undergoes myristoylation, but not palmitoylation in vitro. Removal of the N-terminal myristate acceptor site partially reduced McCPK1 plasma membrane (PM) localization as determined by transient expression of green fluorescent protein fusions in microprojectile-bombarded cells. Removal of the N-terminal domain (amino acids 1-70) completely abolished PM localization, suggesting that myristoylation and possibly the N-terminal domain contribute to membrane association of the kinase. The recombinant, Escherichia coli-expressed, full-length McCPK1 protein was catalytically active in a calcium-dependent manner (K0.5 = 0.15 microm). Autophosphorylation of recombinant McCPK1 was observed in vitro on at least two different Ser residues, with the location of two sites being mapped to Ser-62 and Ser-420. An Ala substitution at the Ser-62 or Ser-420 autophosphorylation site resulted in a slight increase in kinase activity relative to wild-type McCPK1 against a histone H1 substrate. In contrast, Ala substitutions at both sites resulted in a dramatic decrease in kinase activity relative to wild-type McCPK1 using histone H1 as substrate. McCPK1 undergoes a reversible change in subcellular localization from the PM to the nucleus, endoplasmic reticulum, and actin microfilaments of the cytoskeleton in response to reductions in humidity, as determined by transient expression of McCPK1-green fluorescent protein fusions in microprojectile-bombarded cells and confirmed by subcellular fractionation and western-blot analysis of 6x His-tagged McCPK1.

Indexed as

Base SequenceCyclic AMP-Dependent Protein KinasesDesiccationDNA PrimersMagnoliopsidaMolecular Sequence DataOsmolar ConcentrationPhosphorylationSodium ChlorideSubcellular FractionsTransfectionCyclic AMP-Dependent Protein KinasesDNA PrimersSodium Chloride

Identifiers

PMID15247393
PMCPMC519060
OpenAlexW2163638836

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.