Evidence map›Paper›PMID 30012094›Full record

ArticleBMC plant biology2018

Phosphorylation of Arabidopsis SINA2 by CDKG1 affects its ubiquitin ligase activity.

Yang Chen, Mohamed Fokar, Miyoung Kang, Naichong Chen, Randy D Allen, Yaofeng Chen

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

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  9. A CRISPR/Cas9-Based Mutagenesis Protocol forFrontiers in plant science · 2020
    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

6 authors at 2 institutions in 2 countries.

Yang ChenCollege of Agriculture, Northwest Agriculture and Forestry University, Yangling, Shaanxi, 712100, Republic of China.
Mohamed FokarInstitute for Agricultural Biosciences, Oklahoma State University, Ardmore, OK, 73401, USA.
Miyoung KangInstitute for Agricultural Biosciences, Oklahoma State University, Ardmore, OK, 73401, USA.
Naichong ChenInstitute for Agricultural Biosciences, Oklahoma State University, Ardmore, OK, 73401, USA.
Randy D AllenInstitute for Agricultural Biosciences, Oklahoma State University, Ardmore, OK, 73401, USA. randy.allen@okstate.edu.
Yaofeng ChenCollege of Agriculture, Northwest Agriculture and Forestry University, Yangling, Shaanxi, 712100, Republic of China. chenyf3828@126.com.
Oklahoma State University Institute of Technology · USNorthwest A&F University · CN

Funding

China Scholarship Council 201406300140National Institute of Food and Agriculture 2004-35304-15002
6 · The paper itself

Abstract

backgroundSEVEN IN ABSENTIA (SINA) is a RING domain-containing ubiquitin ligase involved in Drosophila eye formation. SINA-like proteins in plants are involved in several signaling pathways. Of the 18 SINA-like proteins identified in Arabidopsis, SEVEN IN ABSENTIA 2 (SINA2) lacks a canonical RING domain and is thought to lack ubiquitin ligase activity.

resultsOur results show that SINA2 has E3 ligase activity in vitro, raising the possibility that a modified B-box domain may compensate for its lack of a RING domain. SINA2 physically interacts with the nuclear protein CYCLIN-DEPENDENT KINASE G1 (CDKG1), which acts as a positive regulator of plant responses to abiotic stress. CDKG1 is expressed in multiple tissues and its expression increased in response to abscisic acid (ABA) and osmotic stress. Transgenic Arabidopsis plants that ectopically express CDKG1 exhibit increased tolerance to ABA and osmotic stress treatments during seed germination and cotyledon development, while the loss-of-function cdkg1 mutant plants show reduced tolerance to ABA and osmotic stress treatments. Moreover, CDKG1-dependent phosphorylation of SINA2 positively affects its E3 ubiquitin ligase activity.

conclusionsBased on these results, we propose that CDKG1 modulates SINA2 ubiquitin ligase activity to regulate its effect on plant responses to ABA and osmotic stress.

Indexed as

Abscisic AcidArabidopsisArabidopsis ProteinsCyclin-Dependent KinasesIntracellular Signaling Peptides and ProteinsOsmotic PressurePhosphorylationPlant Growth RegulatorsPlants, Genetically ModifiedAbscisic AcidArabidopsis ProteinsCDKG1 protein, ArabidopsisCyclin-Dependent KinasesIntracellular Signaling Peptides and ProteinsPlant Growth RegulatorsSINA2 protein, ArabidopsisCDKG1PhosphorylationSINA2Stress responseUbiquitin ligase activity

Identifiers

PMID30012094
PMCPMC6048857
OpenAlexW2884889375

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.