Evidence map›Paper›PMID 18676877›Full record

ArticleThe Plant cell2008

Arabidopsis protein disulfide isomerase-5 inhibits cysteine proteases during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds.

Christine Andème Ondzighi, David A Christopher, Eun Ju Cho, Shu-Choeng Chang, L Andrew Staehelin

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2008. 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
10.8field-weighted citation impact, top 2% 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, 171 citations in OpenAlex.

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  12. Expression Characterization ofInternational journal of molecular sciences · 2022
    Article
  13. Interference of ArabidopsisFrontiers in plant science · 2022
    Article
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12 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Christine Andème OndzighiMolecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347, USA. ondzighi@colorado.edu
David A Christopher
Eun Ju Cho
Shu-Choeng Chang
L Andrew Staehelin
University of Hawaii System · USUniversity of Colorado Boulder · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein disulfide isomerase (PDI) oxidizes, reduces, and isomerizes disulfide bonds, modulates redox responses, and chaperones proteins. The Arabidopsis thaliana genome contains 12 PDI genes, but little is known about their subcellular locations and functions. We demonstrate that PDI5 is expressed in endothelial cells about to undergo programmed cell death (PCD) in developing seeds. PDI5 interacts with three different Cys proteases in yeast two-hybrid screens. One of these traffics together with PDI5 from the endoplasmic reticulum through the Golgi to vacuoles, and its recombinant form is functionally inhibited by recombinant PDI5 in vitro. Peak PDI5 expression in endothelial cells precedes PCD, whereas decreasing PDI5 levels coincide with the onset of PCD-related cellular changes, such as enlargement and subsequent collapse of protein storage vacuoles, lytic vacuole shrinkage and degradation, and nuclear condensation and fragmentation. Loss of PDI5 function leads to premature initiation of PCD during embryogenesis and to fewer, often nonviable, seeds. We propose that PDI5 is required for proper seed development and regulates the timing of PCD by chaperoning and inhibiting Cys proteases during their trafficking to vacuoles before PCD of the endothelial cells. During this transitional phase of endothelial cell development, the protein storage vacuoles become the de facto lytic vacuoles that mediate PCD.

Indexed as

Amino Acid SequenceApoptosisArabidopsisArabidopsis ProteinsCysteine EndopeptidasesElectrophoresis, Polyacrylamide GelImmunoblottingMicroscopy, Electron, TransmissionMolecular Sequence DataPlants, Genetically ModifiedProtein Disulfide-IsomerasesProtein TransportReverse Transcriptase Polymerase Chain ReactionSeedsTwo-Hybrid System TechniquesVacuolesArabidopsis ProteinsCysteine EndopeptidasesProtein Disulfide-Isomerases

Identifiers

PMID18676877
PMCPMC2553623
OpenAlexW2142379034

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.