Evidence map›Paper›PMID 26824478›Full record

ArticlePloS one2016

The Early-Acting Peroxin PEX19 Is Redundantly Encoded, Farnesylated, and Essential for Viability in Arabidopsis thaliana.

Margaret M McDonnell, Sarah E Burkhart, Jerrad M Stoddard, Zachary J Wright, Lucia C Strader, Bonnie Bartel

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
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  8. APlant direct · 2019
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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

6 authors at 2 institutions in 1 country.

Margaret M McDonnellDepartment of BioSciences, Rice University, Houston, Texas, United States of America.
Sarah E BurkhartDepartment of BioSciences, Rice University, Houston, Texas, United States of America.
Jerrad M StoddardDepartment of BioSciences, Rice University, Houston, Texas, United States of America.
Zachary J WrightDepartment of BioSciences, Rice University, Houston, Texas, United States of America.
Lucia C StraderDepartment of Biology, Washington University at St. Louis, St. Louis, Missouri, United States of America.
Bonnie BartelDepartment of BioSciences, Rice University, Houston, Texas, United States of America.
Rice University · USWashington University in St. Louis · US

Funding

Laser scanning confocal microscopeS10RR026399 · NCRR · RICE UNIVERSITY · PI BARTEL, BONNIE · 2010 to 2010
$500k
NCRR NIH HHS S10 RR026399NCRR NIH HHS S10RR026399-01
6 · The paper itself

Abstract

Peroxisomes are single-membrane bound organelles that are essential for normal development in plants and animals. In mammals and yeast, the peroxin (PEX) proteins PEX3 and PEX19 facilitate the early steps of peroxisome membrane protein (PMP) insertion and pre-peroxisome budding from the endoplasmic reticulum. The PEX3 membrane protein acts as a docking site for PEX19, a cytosolic chaperone for PMPs that delivers PMPs to the endoplasmic reticulum or peroxisomal membrane. PEX19 is farnesylated in yeast and mammals, and we used immunoblotting with prenylation mutants to show that PEX19 also is fully farnesylated in wild-type Arabidopsis thaliana plants. We examined insertional alleles disrupting either of the two Arabidopsis PEX19 isoforms, PEX19A or PEX19B, and detected similar levels of PEX19 protein in the pex19a-1 mutant and wild type; however, PEX19 protein was nearly undetectable in the pex19b-1 mutant. Despite the reduction in PEX19 levels in pex19b-1, both pex19a-1 and pex19b-1 single mutants lacked notable peroxisomal β-oxidation defects and displayed normal levels and localization of peroxisomal matrix and membrane proteins. The pex19a-1 pex19b-1 double mutant was embryo lethal, indicating a redundantly encoded critical role for PEX19 during embryogenesis. Expressing YFP-tagged versions of either PEX19 isoform rescued this lethality, confirming that PEX19A and PEX19B act redundantly in Arabidopsis. We observed that pex19b-1 enhanced peroxisome-related defects of a subset of peroxin-defective mutants, supporting a role for PEX19 in peroxisome function. Together, our data indicate that Arabidopsis PEX19 promotes peroxisome function and is essential for viability.

Indexed as

Gene Expression Regulation, PlantProtein Processing, Post-TranslationalAmino Acid SequenceArabidopsisArabidopsis ProteinsBacterial ProteinsEndoplasmic ReticulumGenes, LethalGenes, ReporterLuminescent ProteinsMembrane ProteinsMolecular Sequence DataMutationPeroxinsPeroxisomesPhylogenyArabidopsis ProteinsBacterial ProteinsLuminescent ProteinsMembrane ProteinsPeroxinsPEX19 protein, ArabidopsisPex3 protein, ArabidopsisProtein Isoformsyellow fluorescent protein, Bacteria

Identifiers

PMID26824478
PMCPMC4733102
OpenAlexW2271588670

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.