Evidence map›Paper›PMID 19961900›Full record

ReviewBiochimica et biophysica acta2010

O-GlcNAc protein modification in plants: Evolution and function.

Neil E Olszewski, Christopher M West, Slim O Sassi, Lynn M Hartweck

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

90 citing papers in PubMed, 154 citations in OpenAlex.

  1. CDK8 phosphorylation of DELLA limits Mediator recruitment in gibberellin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  8. Genome ofProceedings of the National Academy of Sciences of the United States of America · 2024
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30 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

4 authors at 4 institutions in 2 countries.

Neil E OlszewskiDepartment of Plant Biology, Microbial and Plant Genomics Institute, 250 Biological Sciences Center, 1445 Gortner Ave., St. Paul, MN 55108, USA. neil@umn.edu
Christopher M West
Slim O Sassi
Lynn M Hartweck
Department of Plant Biology · USHarvard University Press · USNHS Blood and Transplant · GBUniversity of Oklahoma · US

Funding

Transfer of 5R01GM037539 - 22 CYTOSOLIC PROLINE HYDROXYLATION AND GLYCOSYLATIONR01GM037539 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI WEST, CHRISTOPHER M. · 1986 to 2016
$4.4M
NIGMS NIH HHS R01 GM037539NIGMS NIH HHS R01 GM37539
6 · The paper itself

Abstract

The role in plants of posttranslational modification of proteins with O-linked N-acetylglucosamine and the evolution and function of O-GlcNAc transferases responsible for this modification are reviewed. Phylogenetic analysis of eukaryotic O-GlcNAc transferases (OGTs) leads us to propose that plants have two distinct OGTs, SEC- and SPY-like, that originated in prokaryotes. Animals and some fungi have a SEC-like enzyme while plants have both. Green algae and some members of the Apicomplexa and amoebozoa have the SPY-like enzyme. Interestingly the progenitor of the Apicomplexa lineage likely had a photosynthetic plastid that persists in a degenerated form in some species, raising the possibility that plant SPY-like OGTs are derived from a photosynthetic endosymbiont. OGTs have multiple tetratricopeptide repeats (TPRs) that within the SEC- and SPY-like classes exhibit evidence of strong selective pressure on specific repeats, suggesting that the function of these repeats is conserved. SPY-like and SEC-like OGTs have both unique and overlapping roles in the plant. The phenotypes of sec and spy single and double mutants indicate that O-GlcNAc modification is essential and that it affects diverse plant processes including response to hormones and environmental signals, circadian rhythms, development, intercellular transport and virus infection. The mechanistic details of how O-GlcNAc modification affects these processes are largely unknown. A major impediment to understanding this is the lack of knowledge of the identities of the modified proteins.

Indexed as

Evolution, MolecularAcetylglucosamineAmino Acid SequenceArabidopsis ProteinsN-AcetylglucosaminyltransferasesPhylogenyPlantsProtein Processing, Post-TranslationalProtein Structure, TertiaryRepetitive Sequences, Amino AcidRepressor ProteinsSequence AlignmentAcetylglucosamineArabidopsis ProteinsGI protein, ArabidopsisN-AcetylglucosaminyltransferasesO-GlcNAc transferaseRepressor ProteinsSCR protein, ArabidopsisSECRET AGENT protein, ArabidopsisSPY protein, Arabidopsis

Identifiers

PMID19961900
PMCPMC2815191
OpenAlexW2035124967

What OpenQuestion holds

Textmetadata
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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.