Evidence map›Paper›PMID 27306451›Full record

ArticlePlanta2016

Phosphoenolpyruvate carboxylase (PEPC) and PEPC-kinase (PEPC-k) isoenzymes in Arabidopsis thaliana: role in control and abiotic stress conditions.

Ana B Feria, Nadja Bosch, Alfonso Sánchez, Ana I Nieto-Ingelmo, Clara de la Osa, Cristina Echevarría, Sofía García-Mauriño, Jose Antonio Monreal

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Ana B FeriaDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Nadja BoschDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Alfonso SánchezDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Ana I Nieto-IngelmoDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Clara de la OsaDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Cristina EchevarríaDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Sofía García-MauriñoDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain.
Jose Antonio MonrealDepartamento de Biología Vegetal y Ecología, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes no. 6, 41012, Seville, Spain. monreal@us.es.
Universidad de Sevilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MAIN

conclusionArabidopsis ppc3 mutant has a growth-arrest phenotype and is affected in phosphate- and salt-stress responses, showing that this protein is crucial under control or stress conditions. Phosphoenolpyruvate carboxylase (PEPC) and its dedicated kinase (PEPC-k) are ubiquitous plant proteins implicated in many physiological processes. This work investigates specific roles for the three plant-type PEPC (PTPC) and the two PEPC-k isoenzymes in Arabidopsis thaliana. The lack of any of the PEPC isoenzymes reduced growth parameters under optimal growth conditions. PEPC activity was decreased in shoots and roots of ppc2 and ppc3 mutants, respectively. Phosphate starvation increased the expression of all PTPC and PPCK genes in shoots, but only PPC3 and PPCK2 in roots. The absence of any of these two proteins was not compensated by other isoforms in roots. The effect of salt stress on PTPC and PPCK expression was modest in shoots, but PPC3 was markedly increased in roots. Interestingly, both stresses decreased root growth in each of the mutants except for ppc3. This mutant had a stressed phenotype in control conditions (reduced root growth and high level of stress molecular markers), but was unaffected in their response to high salinity. Salt stress increased PEPC activity, its phosphorylation state, and L-malate content in roots, all these responses were abolished in the ppc3 mutant. Our results highlight the importance of the PPC3 isoenzyme for the normal development of plants and for root responses to stress.

Indexed as

MutationArabidopsisArabidopsis ProteinsBlotting, WesternGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicGene Expression Regulation, PlantIsoenzymesPhosphatesPhosphoenolpyruvate CarboxylasePlant RootsPlant ShootsProtein Serine-Threonine KinasesReverse Transcriptase Polymerase Chain ReactionSalinityStress, PhysiologicalArabidopsis ProteinsIsoenzymesPhosphatesPhosphoenolpyruvate Carboxylasephosphoenolpyruvate carboxylase kinaseProtein Serine-Threonine KinasesAnaplerotic functionPhosphate starvationProtein kinaseSalt stress

Identifiers

PMID27306451
OpenAlexW2429714364

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.