Evidence map›Paper›PMID 22430844›Full record

ArticlePlant physiology2012

Isolation and proteomic characterization of the Arabidopsis Golgi defines functional and novel components involved in plant cell wall biosynthesis.

Harriet T Parsons, Katy Christiansen, Bernhard Knierim, Andrew Carroll, Jun Ito, Tanveer S Batth, Andreia M Smith-Moritz, Stephanie Morrison, Peter McInerney, Masood Z Hadi and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
24.9field-weighted citation impact, top 1% 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

95 citing papers in PubMed, 181 citations in OpenAlex.

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  8. ACS omega · 2024
    Article
  9. Review
  10. 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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35 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

16 authors at 4 institutions in 1 country.

Harriet T ParsonsJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Katy Christiansen
Bernhard Knierim
Andrew Carroll
Jun Ito
Tanveer S Batth
Andreia M Smith-Moritz
Stephanie Morrison
Peter McInerney
Masood Z Hadi
Manfred Auer
Aindrila Mukhopadhyay
Christopher J Petzold
Henrik V Scheller
Dominique Loqué
Joshua L Heazlewood
Joint BioEnergy Institute · USSandia National Laboratories California · USLawrence Berkeley National Laboratory · USUniversity of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plant Golgi plays a pivotal role in the biosynthesis of cell wall matrix polysaccharides, protein glycosylation, and vesicle trafficking. Golgi-localized proteins have become prospective targets for reengineering cell wall biosynthetic pathways for the efficient production of biofuels from plant cell walls. However, proteomic characterization of the Golgi has so far been limited, owing to the technical challenges inherent in Golgi purification. In this study, a combination of density centrifugation and surface charge separation techniques have allowed the reproducible isolation of Golgi membranes from Arabidopsis (Arabidopsis thaliana) at sufficiently high purity levels for in-depth proteomic analysis. Quantitative proteomic analysis, immunoblotting, enzyme activity assays, and electron microscopy all confirm high purity levels. A composition analysis indicated that approximately 19% of proteins were likely derived from contaminating compartments and ribosomes. The localization of 13 newly assigned proteins to the Golgi using transient fluorescent markers further validated the proteome. A collection of 371 proteins consistently identified in all replicates has been proposed to represent the Golgi proteome, marking an appreciable advancement in numbers of Golgi-localized proteins. A significant proportion of proteins likely involved in matrix polysaccharide biosynthesis were identified. The potential within this proteome for advances in understanding Golgi processes has been demonstrated by the identification and functional characterization of the first plant Golgi-resident nucleoside diphosphatase, using a yeast complementation assay. Overall, these data show key proteins involved in primary cell wall synthesis and include a mixture of well-characterized and unknown proteins whose biological roles and importance as targets for future research can now be realized.

Indexed as

ApyraseArabidopsisArabidopsis ProteinsBase SequenceCell WallCentrifugation, Density GradientChromatography, LiquidEnzyme AssaysGenes, PlantGenetic Complementation TestGlycosylationGolgi ApparatusImmunoblottingIntracellular MembranesMicroscopy, Electron, TransmissionMolecular Sequence DataAPY1 protein, ArabidopsisApyraseArabidopsis Proteinsguanosine-diphosphataseProteomePyrophosphatases

Identifiers

PMID22430844
PMCPMC3375956
OpenAlexW2166955792

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.