Evidence map›Paper›PMID 31232446›Full record

ArticleJournal of experimental botany2019

CEPR2 phosphorylates and accelerates the degradation of PYR/PYLs in Arabidopsis.

Zipeng Yu, Di Zhang, Yang Xu, Songsong Jin, Lei Zhang, Shizhong Zhang, Guodong Yang, Jinguang Huang, Kang Yan, Changai Wu and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
15.7field-weighted citation impact, top 1% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 92 citations in OpenAlex.

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  18. Transcription Factor SiDi19-3 Enhances Salt Tolerance of Foxtail Millet andInternational journal of molecular sciences · 2023
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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

11 authors at 1 institution in 1 country.

Zipeng YuState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Di ZhangState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Yang XuState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Songsong JinState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Lei ZhangState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Shizhong ZhangState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Guodong YangState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Jinguang HuangState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Kang YanState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Changai WuState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Chengchao ZhengState Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, China.
Shandong Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyrabactin resistance 1 (PYR1)/PYR1-like (PYL) abscisic acid (ABA) receptors have been proved to be recruited in the plasma membrane (PM). In order to explain the roles of PYR/PYLs in the PM, PYL4 was used as bait to screen the PM-localized leucine-rich repeat receptor-like kinase family, and five members were found directly interacting with PYL4. Loss of function by T-DNA insertion in C-terminally encoded peptide receptor 2 (CEPR2) together with phloem intercalated with xylem (PXY) and PXY-Like 2 (PXL2) led to ABA hypersensitivity, while CEPR2 overexpression led to ABA insensitivity compared with the wild type, indicating the redundant and negative roles of CEPR2, PXY, and PXL2 in ABA signaling. The PYL4 proteins were strongly accumulated in cepr2/pxy/pxl2 compared with the wild type. Furthermore, higher phosphorylation levels accompanied by lower protein levels of PYL4 in CEPR2 overexpression lines were observed, indicating the requirement of phosphorylation of PYLs for degradation. Subsequently, MS and in vitro kinase assays demonstrated that CEPR2 phosphorylated PYL4 at Ser54, while this phosphorylation was diminished or even eliminated in the presence of ABA. Taken together, CEPR2 promotes the phosphorylation and degradation of PYLs in unstressed conditions, whereas ABA represses this process to initiate ABA response during times of stress.

Indexed as

Abscisic AcidArabidopsisArabidopsis ProteinsPhosphorylationProtein KinasesReceptors, Cell SurfaceReceptors, PeptideAbscisic AcidArabidopsis ProteinsCEPR2 protein, ArabidopsisMDIS1 protein, ArabidopsisProtein KinasesPXY protein, ArabidopsisReceptors, Cell SurfaceReceptors, PeptideAbscisic acidCEPR2degradationphosphorylationplasma membranePYR/PYLs

Identifiers

PMID31232446
PMCPMC6793440
OpenAlexW2969673725

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LicenceCC BY-NC
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Registered trials

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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.