Evidence map›Paper›PMID 23424245›Full record

ArticleThe Plant cell2013

Arabidopsis CSN5B interacts with VTC1 and modulates ascorbic acid synthesis.

Juan Wang, Yanwen Yu, Zhijin Zhang, Ruidang Quan, Haiwen Zhang, Ligeng Ma, Xing Wang Deng, Rongfeng Huang

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
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

72 citing papers in PubMed, 154 citations in OpenAlex.

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12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Juan WangBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Yanwen Yu
Zhijin Zhang
Ruidang Quan
Haiwen Zhang
Ligeng Ma
Xing Wang Deng
Rongfeng Huang
Chinese Academy of Agricultural Sciences · CNBiotechnology Research Institute · CNCapital Normal University · CNYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Light regulates ascorbic acid (AsA) synthesis, which increases in the light, presumably reflecting a need for antioxidants to detoxify reactive molecules produced during photosynthesis. Here, we examine this regulation in Arabidopsis thaliana and find that alterations in the protein levels of the AsA biosynthetic enzyme GDP-Man pyrophosphorylase (VTC1) are associated with changes in AsA contents in light and darkness. To find regulatory factors involved in AsA synthesis, we identified VTC1-interacting proteins by yeast two-hybrid screening of a cDNA library from etiolated seedlings. This screen identified the photomorphogenic factor COP9 signalosome subunit 5B (CSN5B), which interacted with the N terminus of VTC1 in yeast and plants. Gel filtration profiling showed that VTC1-CSN5B also associated with the COP9 signalosome complex, and this interaction promotes ubiquitination-dependent VTC1 degradation through the 26S proteasome pathway. Consistent with this, csn5b mutants showed very high AsA levels in both light and darkness. Also, a double mutant of csn5b with the partial loss-of-function mutant vtc1-1 contained AsA levels between those of vtc1-1 and csn5b, showing that CSN5B modulates AsA synthesis by affecting VTC1. In addition, the csn5b mutant showed higher tolerance to salt, indicating that CSN5B regulation of AsA synthesis affects the response to salt stress. Together, our data reveal a regulatory role of CSN5B in light-dark regulation of AsA synthesis.

Indexed as

ArabidopsisArabidopsis ProteinsAscorbic AcidCOP9 Signalosome ComplexDarknessLightMultiprotein ComplexesMutationNucleotidyltransferasesOxidative StressPeptide HydrolasesPlants, Genetically ModifiedProteasome Endopeptidase ComplexSalt ToleranceSeedlingsTwo-Hybrid System TechniquesArabidopsis ProteinsAscorbic AcidATP dependent 26S proteaseCOP9 Signalosome ComplexCOP9 signalosome subunit 5, Arabidopsismannose 1-phosphate guanylyltransferaseMultiprotein ComplexesNucleotidyltransferasesPeptide HydrolasesProteasome Endopeptidase Complex

Identifiers

PMID23424245
PMCPMC3608782
OpenAlexW2104097393

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.