Evidence map›Paper›PMID 22021414›Full record

ArticleThe Plant cell2011

Single cystathionine β-synthase domain-containing proteins modulate development by regulating the thioredoxin system in Arabidopsis.

Kyoung Shin Yoo, Sung Han Ok, Byung-Cheon Jeong, Kwang Wook Jung, Mei Hua Cui, Sujin Hyoung, Myeong-Ryeol Lee, Hyun Kyu Song, Jeong Sheop Shin

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

54 citing papers in PubMed, 121 citations in OpenAlex.

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  12. NewAntioxidants (Basel, Switzerland) · 2022
    Article
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  16. Genetic Conservation of CBS Domain Containing Protein Family inInternational journal of molecular sciences · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Kyoung Shin YooSchool of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea. skysini@korea.ac.kr
Sung Han Ok
Byung-Cheon Jeong
Kwang Wook Jung
Mei Hua Cui
Sujin Hyoung
Myeong-Ryeol Lee
Hyun Kyu Song
Jeong Sheop Shin
Korea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant thioredoxins (Trxs) participate in two redox systems found in different cellular compartments: the NADP-Trx system (NTS) in the cytosol and mitochondria and the ferredoxin-Trx system (FTS) in the chloroplast, where they function as redox regulators by regulating the activity of various target enzymes. The identities of the master regulators that maintain cellular homeostasis and modulate timed development through redox regulating systems have remained completely unknown. Here, we show that proteins consisting of a single cystathionine β-synthase (CBS) domain pair stabilize cellular redox homeostasis and modulate plant development via regulation of Trx systems by sensing changes in adenosine-containing ligands. We identified two CBS domain-containing proteins in Arabidopsis thaliana, CBSX1 and CBSX2, which are localized to the chloroplast, where they activate all four Trxs in the FTS. CBSX3 was found to regulate mitochondrial Trx members in the NTS. CBSX1 directly regulates Trxs and thereby controls H(2)O(2) levels and regulates lignin polymerization in the anther endothecium. It also affects plant growth by regulating photosynthesis-related [corrected] enzymes, such as malate dehydrogenase, via homeostatic regulation of Trxs. Based on our findings, we suggest that the CBSX proteins (or a CBS pair) are ubiquitous redox regulators that regulate Trxs in the FTS and NTS to modulate development and maintain homeostasis under conditions that are threatening to the cell.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsCotyledonCystathionine beta-SynthaseFlowersGene Expression Regulation, PlantHomeostasisHydrogen PeroxideLigninModels, MolecularMolecular Sequence DataMutagenesis, InsertionalOxidation-ReductionProtein Structure, SecondaryProtein Structure, TertiaryArabidopsis ProteinsCBSX2 protein, ArabidopsisCDCP2 protein, ArabidopsisCystathionine beta-SynthaseHydrogen PeroxideLigninThioredoxins

Identifiers

PMID22021414
PMCPMC3229136
OpenAlexW2163822036

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.