Evidence map›Paper›PMID 25724641›Full record

ArticleThe Plant cell2015

The rice CK2 kinase regulates trafficking of phosphate transporters in response to phosphate levels.

Jieyu Chen, Yifeng Wang, Fei Wang, Jian Yang, Mingxing Gao, Changying Li, Yingyao Liu, Yu Liu, Naoki Yamaji, Jian Feng Ma and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
13.4field-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

68 citing papers in PubMed, 179 citations in OpenAlex.

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  8. Post-Translational Modifications of TOE3 Regulate Antiviral Defense in Tobacco.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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8 more citing papers are in PubMed but not listed here.

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

16 authors at 5 institutions in 4 countries.

Jieyu ChenState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Yifeng WangState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Fei WangState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Jian YangState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Mingxing GaoState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Changying LiState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Yingyao LiuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Yu LiuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Naoki YamajiInstitute of Plant Science and Resources, Okayama University, Kurashiki 710-0046, Japan.
Jian Feng MaInstitute of Plant Science and Resources, Okayama University, Kurashiki 710-0046, Japan.
Javier Paz-AresCentro Nacional de Biotecnologia, Consejo Superior de Investigaciones Científicas, Campus de Cantoblanco, 28049 Madrid, Spain.
Laurent NussaumeUnité Mixte de Recherche 7265 Commissariat à l'Energie Atomique/CNRS/University of Aix-Marseille, Institute for Biotechnology and Environmental Biology/SBVME/Laboratory of Plant Development Biology, Commissariat à l'Energie Atomique, Cadarache, St. Paul lez Durance F-13108, France.
Shuqun ZhangState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
Keke YiState Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control, Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, China Key Laboratory of Plant Nutrition and Fertilizer, Ministry of Agriculture, Institute of Agricultural Resources and Regional Planning, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Zhongchang WuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China wzchang@zju.edu.cn.ORCID http://orcid.org/0000-0001-6383-3817
Ping WuState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310058, China.
State Key Laboratory of Plant Physiology and BiochemistryOkayama University · JPCentre National de la Recherche Scientifique · FRConsejo Superior de Investigaciones Científicas · ESInstitute of Agricultural Resources and Regional Planning · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphate transporters (PTs) mediate phosphorus uptake and are regulated at the transcriptional and posttranslational levels. In one key mechanism of posttranslational regulation, phosphorylation of PTs affects their trafficking from the endoplasmic reticulum (ER) to the plasma membrane. However, the kinase(s) mediating PT phosphorylation and the mechanism leading to ER retention of phosphorylated PTs remain unclear. In this study, we identified a rice (Oryza sativa) kinase subunit, CK2β3, which interacts with PT2 and PT8 in a yeast two-hybrid screen. Also, the CK2α3/β3 holoenzyme phosphorylates PT8 under phosphate-sufficient conditions. This phosphorylation inhibited the interaction of PT8 with PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1, a key cofactor regulating the exit of PTs from the ER to the plasma membrane. Additionally, phosphorus starvation promoted CK2β3 degradation, relieving the negative regulation of PT phosphorus-insufficient conditions. In accordance, transgenic expression of a nonphosphorylatable version of OsPT8 resulted in elevated levels of that protein at the plasma membrane and enhanced phosphorus accumulation and plant growth under various phosphorus regimes. Taken together, these results indicate that CK2α3/β3 negatively regulates PTs and phosphorus status regulates CK2α3/β3.

Indexed as

Casein Kinase IICell MembraneEndoplasmic ReticulumModels, BiologicalMutationOryzaPhenotypePhosphatesPhosphate Transport ProteinsPhosphorylationPlant ProteinsPlants, Genetically ModifiedProtein BindingProtein TransportSerineCasein Kinase IIPhosphatesPhosphate Transport ProteinsPlant ProteinsSerine

Identifiers

PMID25724641
PMCPMC4558666
OpenAlexW2120396983

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.