Evidence map›Paper›PMID 23104112›Full record

ArticlePlant signaling & behavior2013

Multifaceted roles of Arabidopsis PP6 phosphatase in regulating cellular signaling and plant development.

Mingqiu Dai, William Terzaghi, Haiyang Wang

Open access · bronzeAbstract read
In one paragraph

Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Alternative splicing in tomato pollen in response to heat stress.DNA research : an international journal for rapid publication of reports on genes and genomes · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
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

3 authors at 3 institutions in 3 countries.

Mingqiu DaiDepartment of Molecular, Cellular, and Developmental Biology; Yale University; New Haven, CT USA.
William TerzaghiDepartment of Molecular, Cellular, and Developmental Biology; Yale University; New Haven, CT USA; Department of Biology; Wilkes University; Wilkes-Barre, PA USA.
Haiyang WangDepartment of Molecular, Cellular, and Developmental Biology; Yale University; New Haven, CT USA; National Engineering Research Center for Crop Molecular Design; Beijing, China; Institute of Crop Sciences; Chinese Academy of Agriculture Sciences; Beijing, China; College of Life Science; Capital Normal University; Beijing, China.
Beijing National Laboratory for Molecular Sciences · CNUniversity of New Haven · USYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible protein phosphorylation catalyzed by kinases and phosphatases is a major form of posttranslational regulation that plays a central role in regulating many signaling pathways. While large families of both protein kinases and protein phosphatases have been identified in plants, kinases outnumber phosphatases. This raises the question of how a relatively limited number of protein phosphatases can maintain protein phosphorylation homeostasis in a cell. Recent studies have shown that Arabidopsis FyPP1 (Phytochrome-associated serine/threonine protein phosphatase 1) and FyPP3 encode the catalytic subunits of protein phosphatase 6 (PP6), and that they directly binds to the A subunits of protein phosphatase 2A (PP2AA proteins), and SAL (SAPS domain-like) proteins to form the heterotrimeric PP6 holoenzyme complex. Emerging evidence is suggesting that PP6, acts in opposition with multiple classes of kinases, to regulate the phosphorylation status of diverse substrates and subsequently numerous developmental processes and responses to environmental stimuli.

Indexed as

Gene Expression Regulation, PlantPlant DevelopmentAdaptation, PhysiologicalArabidopsisArabidopsis ProteinsHomeostasisPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2Signal TransductionArabidopsis ProteinsAtFyPP3 protein, ArabidopsisFyPP1 protein, ArabidopsisFyPP protein, ArabidopsisPhosphoprotein PhosphatasesProtein Phosphatase 2protein phosphatase 6ArabidopsisFyPPPP6protein phosphatase

Identifiers

PMID23104112
PMCPMC3745556
OpenAlexW2053170518

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.