Evidence map›Paper›PMID 42711402›Full record

ArticleNature plants2026

An LRR co-receptor kinase essential for systemic nitrogen-demand signalling.

Mari Ogawa-Ohnishi, Taizo Nomura, Yoko Hayashi, Yasuko Yamashita, Saki Noda, Reiji Suda, Yuri Ohkubo, Yoshikatsu Matsubayashi

Abstract read
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In one paragraph

Article in Nature plants, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Mari Ogawa-Ohnishi *Department of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.ORCID http://orcid.org/0000-0002-7581-2607
Taizo Nomura *Department of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
Yoko HayashiDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
Yasuko YamashitaDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
Saki NodaDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
Reiji SudaDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
Yuri OhkuboDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.ORCID http://orcid.org/0000-0001-9228-6293
Yoshikatsu MatsubayashiDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan. matsu@bio.nagoya-u.ac.jp.ORCID http://orcid.org/0000-0002-2669-2119

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) 23H05477MEXT | Japan Society for the Promotion of Science (JSPS) 23K14209MEXT | Japan Society for the Promotion of Science (JSPS) 24K18137MEXT | Japan Society for the Promotion of Science (JSPS) 25H01342
6 · The paper itself

Abstract

Plants have evolved a signalling pathway in which, when one root senses local nitrogen (N) deficiency, nitrate uptake by other roots is enhanced in a complementary manner. This long-range communication, known as systemic N-demand signalling, is triggered when the root-to-shoot mobile signal, C-TERMINALLY ENCODED PEPTIDE (CEP), which is induced in roots under N starvation, is perceived by CEP RECEPTOR 1 (CEPR1) expressed in the leaf phloem. However, the molecular components required for CEP-dependent CEPR1 activation remain unknown. Here we identified a leucine-rich repeat receptor kinase that interacts with CEPR1 in a CEP-dependent manner, which we named CEP RECEPTOR INTERACTOR (CERI). CERI belongs to the last functionally uncharacterized clade within the Arabidopsis leucine-rich repeat receptor kinase subgroup II. Loss of CERI impairs systemic N-demand signalling but does not affect CEPR1-mediated regulation of root system architecture. CERI functions as a co-receptor that confers signalling specificity on CEPR1 by selectively mediating systemic N-demand signalling.

Indexed as

ArabidopsisArabidopsis ProteinsNitrogenProtein KinasesSignal TransductionGene Expression Regulation, PlantPlant RootsReceptors, PeptideArabidopsis ProteinsCEPR1 protein, ArabidopsisNitrogenProtein KinasesReceptors, Peptide

Identifiers

PMID42711402

What OpenQuestion holds

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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.