Evidence map›Paper›PMID 25253886›Full record

ArticlePlant physiology2014

Systematic phenotypic screen of Arabidopsis peroxisomal mutants identifies proteins involved in β-oxidation.

Gaëlle Cassin-Ross, Jianping Hu

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  6. Plant peroxisomal solute transporter proteins.Journal of integrative plant biology · 2019
    Review
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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.

Gaëlle Cassin-RossMichigan State University-Department of Energy Plant Research Laboratory (G.C.-R., J.H.) andPlant Biology Department (J.H.), Michigan State University, East Lansing, Michigan 48824.
Jianping HuMichigan State University-Department of Energy Plant Research Laboratory (G.C.-R., J.H.) andPlant Biology Department (J.H.), Michigan State University, East Lansing, Michigan 48824 huji@msu.edu.
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisomes are highly dynamic and multifunctional organelles essential to development. Plant peroxisomes accommodate a multitude of metabolic reactions, many of which are related to the β-oxidation of fatty acids or fatty acid-related metabolites. Recently, several dozens of novel peroxisomal proteins have been identified from Arabidopsis (Arabidopsis thaliana) through in silico and experimental proteomic analyses followed by in vivo protein targeting validations. To determine the functions of these proteins, we interrogated their transfer DNA insertion mutants with a series of physiological, cytological, and biochemical assays to reveal peroxisomal deficiencies. Sugar dependence and 2,4-dichlorophenoxybutyric acid and 12-oxo-phytodienoic acid response assays uncovered statistically significant phenotypes in β-oxidation-related processes in mutants for 20 of 27 genes tested. Additional investigations uncovered a subset of these mutants with abnormal seed germination, accumulation of oil bodies, and delayed degradation of long-chain fatty acids during early seedling development. Mutants for seven genes exhibited deficiencies in multiple assays, strongly suggesting the involvement of their gene products in peroxisomal β-oxidation and initial seedling growth. Proteins identified included isoforms of enzymes related to β-oxidation, such as acyl-CoA thioesterase2, acyl-activating enzyme isoform1, and acyl-activating enzyme isoform5, and proteins with functions previously unknown to be associated with β-oxidation, such as Indigoidine synthase A, Senescence-associated protein/B12D-related protein1, Betaine aldehyde dehydrogenase, and Unknown protein5. This multipronged phenotypic screen allowed us to reveal β-oxidation proteins that have not been discovered by single assay-based mutant screens and enabled the functional dissection of different isoforms of multigene families involved in β-oxidation.

Indexed as

2,4-Dichlorophenoxyacetic AcidArabidopsisArabidopsis ProteinsCarbohydrate MetabolismFatty AcidsFatty Acids, UnsaturatedGene Expression Regulation, PlantGerminationIsocitrate DehydrogenaseLipid DropletsMembrane ProteinsMutationOxidation-ReductionPeroxisomesPhenotypeRepressor Proteins12-oxophytodienoic acid2,4-Dichlorophenoxyacetic Acid4-(2,4-dichlorophenoxy)butyric acidArabidopsis ProteinsFatty AcidsFatty Acids, UnsaturatedICDH protein, ArabidopsisIsocitrate DehydrogenaseMembrane ProteinsPEX14 protein, ArabidopsisRepressor Proteins

Identifiers

PMID25253886
PMCPMC4226370
OpenAlexW2106978542

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.