Evidence map›Paper›PMID 23443557›Full record

ArticleNature communications2013

S-nitrosylation of phosphotransfer proteins represses cytokinin signaling.

Jian Feng, Chun Wang, Qingguo Chen, Hui Chen, Bo Ren, Xiaoming Li, Jianru Zuo

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed, 1 pooled it
22.6field-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

65 citing papers in PubMed, 1 synthesis or guideline pooled it, 189 citations in OpenAlex.

  1. Pooled it
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  12. De-nitrosylation Coordinates Appressorium Function for Infection of the Rice Blast Fungus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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5 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

7 authors at 3 institutions in 1 country.

Jian FengState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
Chun Wang
Qingguo Chen
Hui Chen
Bo Ren
Xiaoming Li
Jianru Zuo
Institute of Genetics and Developmental Biology · CNChinese Academy of Sciences · CNUniversity of Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytokinin is an essential phytohormone in plant growth and development. In Arabidopsis, cytokinin signalling is mediated by a phosphorelay that sequentially transfers phosphoryl groups from the cytokinin receptors to histidine phosphotransfer proteins (AHPs) and response regulators (ARRs). However, little is known about the regulatory mechanism of the phosphorelay. Here, we show that nitric oxide negatively regulates cytokinin signalling by inhibiting the phosphorelay activity through S-nitrosylation. S-nitrosylation of AHP1 at Cys 115 represses its phosphorylation and subsequent transfer of the phosphoryl group to ARR1. A non-nitrosylatable mutation of AHP1 renders the mutant protein insensitive to nitric oxide in repressing its phosphorylation, and partially relieves the inhibitory effect of nitric oxide on the cytokinin response. Conversely, a nitrosomimetic mutation of AHP1 causes reduced phosphorylation of AHP1 and ARR1, thereby resulting in a compromised cytokinin response. These findings illustrate a mechanism by which redox signalling and cytokinin signalling coordinate plant growth and development.

Indexed as

Signal TransductionArabidopsisArabidopsis ProteinsCell CountCysteineCytokininsDNA-Binding ProteinsHypocotylMutationNitric OxideNitrosationPhosphorylationPhosphotransferasesPlant RootsRecombinant ProteinsS-NitrosoglutathioneAHP1 protein, ArabidopsisArabidopsis ProteinsARR1 protein, ArabidopsisCysteineCytokininsDNA-Binding ProteinsNitric OxidePhosphotransferasesRecombinant ProteinsS-NitrosoglutathioneTranscription Factors

Identifiers

PMID23443557
OpenAlexW1983379119

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.