Evidence map›Paper›PMID 22135470›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Galacturonosyltransferase (GAUT)1 and GAUT7 are the core of a plant cell wall pectin biosynthetic homogalacturonan:galacturonosyltransferase complex.

Melani A Atmodjo, Yumiko Sakuragi, Xiang Zhu, Amy J Burrell, Sushree S Mohanty, James A Atwood, Ron Orlando, Henrik V Scheller, Debra Mohnen

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
–field-weighted citation impact
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

134 citing papers in PubMed.

  1. Review
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  7. Changes in Cell Aggregation inPlants (Basel, Switzerland) · 2025
    Article
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  9. Review
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  17. Impact ofBiotech (Basel (Switzerland)) · 2025
    Article
  18. Review
  19. Article
  20. Review

74 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

9 authors.

Melani A AtmodjoComplex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Yumiko Sakuragi
Xiang Zhu
Amy J Burrell
Sushree S Mohanty
James A Atwood
Ron Orlando
Henrik V Scheller
Debra Mohnen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant cell wall pectic polysaccharides are arguably the most complex carbohydrates in nature. Progress in understanding pectin synthesis has been slow due to its complex structure and difficulties in purifying and expressing the low-abundance, Golgi membrane-bound pectin biosynthetic enzymes. Arabidopsis galacturonosyltransferase (GAUT) 1 is an α-1,4-galacturonosyltransferase (GalAT) that synthesizes homogalacturonan (HG), the most abundant pectic polysaccharide. We now show that GAUT1 functions in a protein complex with the homologous GAUT7. Surprisingly, although both GAUT1 and GAUT7 are type II membrane proteins with single N-terminal transmembrane-spanning domains, the N-terminal region of GAUT1, including the transmembrane domain, is cleaved in vivo. This raises the question of how the processed GAUT1 is retained in the Golgi, the site of HG biosynthesis. We show that the anchoring of GAUT1 in the Golgi requires association with GAUT7 to form the GAUT1:GAUT7 complex. Proteomics analyses also identified 12 additional proteins that immunoprecipitate with the GAUT1:GAUT7 complex. This study provides conclusive evidence that the GAUT1:GAUT7 complex is the catalytic core of an HG:GalAT complex and that cell wall matrix polysaccharide biosynthesis occurs via protein complexes. The processing of GAUT1 to remove its N-terminal transmembrane domain and its anchoring in the Golgi by association with GAUT7 provides an example of how specific catalytic domains of plant cell wall biosynthetic glycosyltransferases could be assembled into protein complexes to enable the synthesis of the complex and developmentally and environmentally plastic plant cell wall.

Indexed as

ArabidopsisArabidopsis ProteinsCell WallGlucuronosyltransferaseGolgi ApparatusImmunoprecipitationModels, BiologicalMultiprotein ComplexesPectinsProtein BindingProtein Processing, Post-TranslationalProteomicsSubstrate SpecificityArabidopsis Proteinsgalacturonosyltransferase 1, Arabidopsisgalacturonosyltransferase 7, ArabidopsisGlucuronosyltransferaseMultiprotein ComplexesPectinspolygalacturonic acid

Identifiers

PMID22135470
PMCPMC3250160

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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.