Evidence map›Paper›PMID 23903947›Full record

ArticlePlant cell reports2013

Arabidopsis CDPK6 phosphorylates ADF1 at N-terminal serine 6 predominantly.

Chun-Hai Dong, Yan Hong

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Article in Plant cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

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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

18 citing papers in PubMed.

  1. Review
  2. Article
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  7. Article
  8. Review
  9. Review
  10. A Decade of Pollen Phosphoproteomics.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. 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.

Chun-Hai DongCollege of Life Sciences, Qingdao Agricultural University, Qingdao, 266109, People's Republic of China, chunhai79@yahoo.com.
Yan Hong

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

key messageWe found that Arabidopsis AtADF1 was phosphorylated by AtCDPK6 at serine 6 predominantly and the phosphoregulation plays a key role in the regulation of ADF1-mediated depolymerization of actin filaments. ABSTRACT: Since actin-depolymerizing factor (ADF) is highly conserved among eukaryotes, it is one of the key modulators for actin organization. In plants, ADF is directly involved in the depolymerization of actin filaments, and therefore important for F-actin-dependent cellular activities. The activity of ADF is tightly controlled through a number of molecular mechanisms, including phosphorylation-mediated inactivation of ADF. To investigate Arabidopsis ADF1 phosphoregulation, we generated AtADF1 phosphorylation site-specific mutants. Using transient expression and stable transgenic approaches, we analyzed the ADF1 phosphorylation mutants in the regulation of actin filament organizations in plant cells. By in vitro phosphorylation assay, we showed that AtADF1 is phosphorylated by AtCDPK6 at serine 6 predominantly. Chemically induced expression of AtCDPK6 can negatively regulate the wild-type AtADF1 in depolymerizing actin filaments, but not those of the mutants AtADF1(S6A) and AtADF1(S6D). These results demonstrate a regulatory function of Arabidopsis CDPK6 in the N-terminal phosphorylation of AtADF1.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsActinsArabidopsisArabidopsis ProteinsBlotting, WesternGreen Fluorescent ProteinsMutant ProteinsMutationPhenotypePhosphorylationPhosphoserinePlant EpidermisPlants, Genetically ModifiedProtein BindingProtein Serine-Threonine KinasesActin Depolymerizing FactorsActinsADF1 protein, ArabidopsisArabidopsis ProteinsCDPK6 protein, ArabidopsisGreen Fluorescent ProteinsMutant ProteinsPhosphoserineProtein Serine-Threonine KinasesRecombinant Fusion Proteins

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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.