Evidence map›Paper›PMID 23512855›Full record

ArticleThe Plant cell2013

14-3-3 regulates 1-aminocyclopropane-1-carboxylate synthase protein turnover in Arabidopsis.

Gyeong Mee Yoon, Joseph J Kieber

Open access · bronzeAbstract 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 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

58 citing papers in PubMed, 119 citations in OpenAlex.

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  7. Journal of agricultural and food chemistry · 2025
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  19. Crosstalk between theInternational journal of molecular sciences · 2022
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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

2 authors at 1 institution in 1 country.

Gyeong Mee YoonDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina 27599-3280, USA.
Joseph J Kieber
University of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

14-3-3 proteins are a family of conserved phospho-specific binding proteins involved in diverse physiological processes. Plants have large 14-3-3 gene families, and many binding partners have been identified, though relatively few functions have been defined. Here, we demonstrate that 14-3-3 proteins interact with multiple 1-aminocyclopropane-1-carboxylate synthase (ACS) isoforms in Arabidopsis thaliana. ACS catalyzes the generally rate-limiting step in the biosynthesis of the phytohormone ethylene. This interaction increases the stability of the ACS proteins. 14-3-3s also interact with the ETHYLENE-OVERPRODUCER1 (ETO1)/ETO1-LIKE (EOLs), a group of three functionally redundant proteins that are components of a CULLIN-3 E3 ubiquitin ligase that target a subset of the ACS proteins for rapid degradation by the 26S proteasome. In contrast with ACS, the interaction with 14-3-3 destabilizes the ETO1/EOLs. The level of the ETO1/EOLs in vivo plays a role in mediating ACS protein turnover, with increased levels leading to a decrease in ACS protein levels. These studies demonstrate that regulation of ethylene biosynthesis occurs by a mechanism in which 14-3-3 proteins act through a direct interaction and stabilization of ACS and through decreasing the abundance of the ubiquitin ligases that target a subset of ACS proteins for degradation.

Indexed as

14-3-3 ProteinsArabidopsisArabidopsis ProteinsBinding SitesEnzyme StabilityEthylenesIntracellular Signaling Peptides and ProteinsIsoenzymesLyasesPeptidesPlants, Genetically ModifiedProteasome Endopeptidase ComplexProtein Interaction MappingProtein TransportProteolysisProtoplasts14-3-3 Proteins1-aminocyclopropanecarboxylate synthaseArabidopsis ProteinsATP dependent 26S proteaseethyleneEthylenesETO1 protein, ArabidopsisIntracellular Signaling Peptides and ProteinsIsoenzymesLyasesPeptidesProteasome Endopeptidase ComplexR18 peptide

Identifiers

PMID23512855
PMCPMC3634674
OpenAlexW2158582211

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.