Evidence map›Paper›PMID 22363620›Full record

ArticlePloS one2012

GO-PROMTO illuminates protein membrane topologies of glycan biosynthetic enzymes in the Golgi apparatus of living tissues.

Casper Søgaard, Anne Stenbæk, Sophie Bernard, Masood Hadi, Azeddine Driouich, Henrik Vibe Scheller, Yumiko Sakuragi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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
4.8field-weighted citation impact, top 5% 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, 21 citations in OpenAlex.

  1. NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  3. Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules that define biological patterns of xyloglucan polymers.Proceedings of the National Academy of Sciences of the United States of America · 2018
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  10. Two Arabidopsis proteins synthesize acetylated xylan in vitro.The Plant journal : for cell and molecular biology · 2014
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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

7 authors at 3 institutions in 3 countries.

Casper SøgaardDepartment of Plant Biology and Biotechnology, Faculty of Life Sciences, University of Copenhagen, Frederiksberg, Denmark.
Anne Stenbæk
Sophie Bernard
Masood Hadi
Azeddine Driouich
Henrik Vibe Scheller
Yumiko Sakuragi
The Velux Foundations · DKJoint BioEnergy Institute · USUniversité de Rouen Normandie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Golgi apparatus is the main site of glycan biosynthesis in eukaryotes. Better understanding of the membrane topology of the proteins and enzymes involved can impart new mechanistic insights into these processes. Publically available bioinformatic tools provide highly variable predictions of membrane topologies for given proteins. Therefore we devised a non-invasive experimental method by which the membrane topologies of Golgi-resident proteins can be determined in the Golgi apparatus in living tissues. A Golgi marker was used to construct a series of reporters based on the principle of bimolecular fluorescence complementation. The reporters and proteins of interest were recombinantly fused to split halves of yellow fluorescent protein (YFP) and transiently co-expressed with the reporters in the Nicotiana benthamiana leaf tissue. Output signals were binary, showing either the presence or absence of fluorescence with signal morphologies characteristic of the Golgi apparatus and endoplasmic reticulum (ER). The method allows prompt and robust determinations of membrane topologies of Golgi-resident proteins and is termed GO-PROMTO (for GOlgi PROtein Membrane TOpology). We applied GO-PROMTO to examine the topologies of proteins involved in the biosynthesis of plant cell wall polysaccharides including xyloglucan and arabinan. The results suggest the existence of novel biosynthetic mechanisms involving transports of intermediates across Golgi membranes.

Indexed as

ArabidopsisArabidopsis ProteinsComputational BiologyGlucansGolgi ApparatusMembrane ProteinsMicroscopy, FluorescenceModels, BiologicalNicotianaOrgan SpecificityPlant LeavesPlants, Genetically ModifiedPolysaccharidesProtein Structure, TertiaryRecombinant Fusion ProteinsReproducibility of ResultsarabanArabidopsis ProteinsGlucansMembrane ProteinsPolysaccharidesRecombinant Fusion ProteinsXylansxyloglucan

Identifiers

PMID22363620
PMCPMC3283625
OpenAlexW2125286218

What OpenQuestion holds

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LicenceCC0
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.